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DIY Animal Plaque Ornaments
Oh, Deer…
Here at REstyleSOURCE, we can always appreciate a unique Christmas tree ornament. After all, there is a history behind them. From traditional ornaments passed down through generations of family, to the one that you won at a white elephant gift exchange party, to baby's first ornament, your Christmas tree has a way of holding all of your family memories and history during the most special time of the year. We love a good variety, however, so it's always nice to make a few of your own ornaments as well! Whether they are fun, goofy, or elegant, we think that everyone should have a few handcrafted ornaments on their tree…which is why we love this DIY project from My Sweet Savannah! Never short on ideas, she found matching deer ornaments at her local thrift store and decided to embellish them in a unique way. While you may not find the same ones, these DIY animal plaque ornaments will work with any little animal trinkets, statues, or ornaments that you are able to find. Put some Christmas tunes on and make an event of it! Materials and instructions listed below.
PHOTO: c/o My Sweet Savannah
Materials Needed:
• Vintage looking scrapbook paper • Pencil • Mod Podge • Sandpaper
• Electric Drill • Annie Sloan Dark Wax • Rag • Ribbon or Twine • Liquid Nails
• Small animal ornaments/trinkets to mount on the plaques (a head will work best)
• Small unfinished wooden shield plaques (can be found at JoAnn Fabrics)
PHOTO: c/o My Sweet Savannah
The first step was to cut the paper to fit the tops of the plaques. I did this by flipping the plaques over and tracing around them with pencil onto the paper and cutting out. Mod podge your paper onto the plaques.
Any excess paper can be sanded off. This step also helps create a worn vintage look.
- Drill holes through the tops of each one so you can hang them as ornaments on your tree.
The next step is to age them. I used Annie Sloan dark wax and a rag, but you can also use stain.Go over the outside edges and smudge it onto the paper a bit as well. Let dry.
Use ribbon, or twine to tie a bow. I used liquid nails to attach the deer to the center of each plaque and let them dry overnight.
- Once they are completely dry, hang them on your tree and admire them!
PHOTO: c/o My Sweet Savannah
PHOTO: c/o My Sweet Savannah


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According to the invitation of the Italian Charity Fund "HELIOS ONLUS" and University medical association AOU "Policlinico - Vittorio Emanuele" di Catania, in collaboration with the Charity Fund Medical Relief, the official delegation of representatives of medical institutions of Ukraine led by
People's deputy of Ukraine
Yuriy Samoilenko visited Catania, Sicily, Italy during 20-28, November 2010.
During the visit, delegation members have had meetings with leaders of several medical institutions, medical faculty of the University, the leading medical specialists.
As a result of the visit signed the agreement on long-term cooperation on the implementation of charitable medical programs whose implementation would improve the quality of medical care to citizens of Ukraine and Italy, will assist in strengthening friendship and cooperation between our peoples.
Meeting at Hospital
Meeting at University
Signing the Agreement
The Agreement
Cooperation in the area of Cardiovascular Surgery

subset: commoncrawl


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I ordered a been and cheese burrito for myself and a tostada for my 4 year old. Neither one of us could eat our meals because of the horrible smelling beans. They literally looked and smelled like vomit. I told the waiter we did not...More
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I ordered a been and cheese burrito for myself and a tostada for my 4 year old. Neither one of us could eat our meals because of the horrible smelling beans. They literally looked and smelled like vomit. I told the waiter we did not...More
This is our favorite place for Mexican in West Omaha. It is billed as Baja Mexican and is not as heavy or oily as other places. The service is very good and the food comes shortly after ordering. Salsa and chips are served when you...More
We have always liked Hector's, but since they have consolidated out West it is even better. The service is very good. We have had Raoul as a waiter for years, and he always remembers us. I had ground beef taquitos the other night and they...More
We went here for a late lunch, and we remembered it to be a decent place. It has gone downhill. I ordered a margarita, enchilada and jalapeno poppers. The margarita was tasty, but food was a fright. My enchilada was good, but small with not...More
Hector's is my wife favorite stop for Mexican food in Omaha. And she's not alone - they are usually busy and often have a waitlist, especially on weekends. The food is good. Service is mostly good although you'll occasionally find a host or server that...More
Being from South Texas, we grew up loving Mexican food. I usually judge a Mexican restaurant by their Chile Rellenos and Guacamole. Hector's Rellenos were great, the Seafood Enchilada was flavorful and my wife's Black Bean Soup was hot, smooth and tasty. Now for the...More
We both ordered Enchiladas Guadalajara. The chicken breast meat was as fresh and tasty as if I has grilled it myself. They were really excellent. As good as I've had anywhere. The chips and salsa were refilled until we said 'no mas". Everything was perfect....More
The salsa was tasteless ..... My meat quesadilla was horrible and greasy and they charged for sour cream ! Beef enchilada sauce was horrific...Everything is extra!! Go anywhere but here....
Recently went to the Hector's in West Omaha. If you haven't been here before, it's definitely worth a stop. To start, you are given chips and salsa. Hector's goes a step further and has a little salsa bar with a couple additional salsas from mild...More
Love the nachos! The grilled chicken tacos are always excellent. My husband loves the burritos. Their Top Shelf Margarita is my favorite one.


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Two hundred beers, an eclectic selection of food, and did we mention desserts?
Live music and valuable coupons – a perfect combination
Check out the latest news at European Street Cafe.
San Marco, Riverside, Southside or the Beach. If you're in Jacksonville, then you're nearby
Written by:
Scared of the dark? Don't be! European Street Cafe in Riverside is bring the best of the dark—to light—on Jan. 25.
As part of The Black Night, we'll be serving black plate special with burnt ends, black pudding and porter cheddar with charcoal crackers (vegetarian option available). There will also be a special S'mores and Graham Cracker Dip. We'll also be featuring a wide variety of dark beers on tap including Veterans United Craft Brewery's Cup of Joe Coffee Oatmeal Stout, Laguintas' Cappuccino Stout, Stone Coffee Milk Stout, Cigar City Oatmeal Raisin Cookie and Evil Twin Imperial Biscotti Break Stout. And we're super excited to tap a keg of the impossible-to-get Underdark 2014 from Intuition Aleworks. We'd tell you how we got it, but then we would have to call your mother a hamster and taunt you a second time … which brings us to the entertainment.
At 7 p.m., grab your coconuts and a seat on the patio for a screening of Monty Python and The Holy Grail, where Arthur battles the Black Knight on his quest to find The Holy Grail.
Throughout the day and night, we've got hourly giveaways, as well as a movie trivia contest where the winner takes own his or own Holy Grail.
We're going to have a raffle to benefit the JB Running Scholarship. Items to be raffled include:
- 12-Pack Sierra Nevada Beer Camp
- 2014 Intuition Underdark Bomber and Cigar City Hunuhpu's
- 2014 Bourbon County Vanilla Rye
- 2013 Samuel Adams Utopia's
Tickets are $5 each or 3 for $10 and are limited to 500 total being sold.
Raffle tickets are on sale at Park Street now. Until then, "Ekki-ekki-ekki-ekki-PTANG. Zoom-Boing, z'nourrwringmm."
Web Design and Web Development by Station Four
Copyright © 2010 European Street Cafe


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Michelle Oseman
The Boss
A born business woman, Michelle's skills include administration, communication, accounts and tea-making. Just don't ask her to go 'paperless'.
Lisa Harris
Lead Trainer
A super talented trainer with the qualifications and awards to prove it. Consumer of vast quantities of crunchy yoghurt and strange teas.
Dean Oseman
Photography & IT
Dean loves taking photographs, playing boxes with strings attached and building websites. Won't do any of this before a cup of tea though.


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Injury to muscle tissue plays a central role in various cardiovascular pathologies. Overexpression of the small heat shock protein Hsp27 protects muscle cells against thermal, oxidative and ischemic stress. However, underlying mechanisms of this protection have not been resolved. A distinctive feature of muscle cells is the stress-induced association of Hsp27 with the sarcomere. The association of Hsp27 with the cytoskeleton, in both muscle and non-muscle cells, is thought to represent interaction with Z-line components or filamentous actin. Here, we examined the association of Hsp27 with myofibrils in adult zebrafish myocardium subjected to hyperthermia and mechanical stretching. Consistent with previously published results, Hsp27 in resting length myofibrils localized to narrowly defined regions, or bands, which colocalized with Z-line markers. However, analysis of stretched myofibrils revealed that the association of Hsp27 with myofibrils was independent of desmin, alpha-actinin, myosin, and filamentous actin. Instead, Hsp27 maintained a consistent relationship with a marker for the titin A/I border over various sarcomeric lengths. Finally, extraction of actin filaments revealed that Hsp27 binds to a component of the remaining sarcomere. Together, these novel data support a mechanism of Hsp27 function where interactions with the titin filament system protect myofibrils from stress-induced degradation.
Heat shock proteins (Hsps) are a large family of proteins, many of which are highly conserved, stress-inducible and confer resistance to various forms of cellular stress and injury. Most Hsps can act as chaperones, assisting the folding of nascent proteins, or preventing irreversible aggregation of proteins following loss of structural integrity. Small heat shock proteins (sHsps) are a distinct subclass of Hsps ranging from 12 to 43 kD in mass [1]. All sHsps are characterized by a C-terminal crystallin domain necessary for dimerization, but sHsps also show considerable diversity in sequence, expression pattern and function [1]. Eleven sHsps have been identified in humans and mice [2], while some species of plants have been shown to express up to nineteen small heat shock protein family members [3].
Hsp27, also known as HspB1, is a widely distributed member of the sHsp family. Hsp27 has been shown to play roles in the preservation of cytoskeletal architecture [4], resistance to oxidative [5,6], thermal and ischemic stress [7,8], protection against heavy metal toxicity [9,10], regulation of cellular redox state [11], and inhibition of cellular apoptotic pathways [12,13]. In addition to stress-inducible expression, Hsp27 is constitutively expressed in many cell types [14–16]. High constitutive expression of Hsp27 is detected in muscle tissues, and thus, its function in striated muscle tissue has received considerable attention. Altered Hsp27 expression has been reported in patients diagnosed with primary desminopathies [17] and following prolonged eccentric exercise in skeletal muscles [18,19]. In cardiomyocytes, Hsp27 overexpression has been correlated with resistance to anthracycline toxicity [20], hypoxia [21], and ischemia/reperfusion injury [7,8,22].
Available data support several mechanisms for Hsp27 cytoprotection of muscle cells. Hsp27 acts as a general chaperone in vitro [23], and overexpression of Hsp27 enhances refolding of fluorescent reporter proteins in the nuclear compartment of fibroblasts [24]. Hsp27 also associates with nuclear speckles in cells subjected to various mechanisms of injury [25–27] and enhances the recovery of RNA splicing activity after experimental heat shock [28]. In addition, Hsp27 has been reported to alter the activity of critical elements of the apoptotic signaling pathways including caspases [29,30], cytochrome c [29,31,32] and Akt [33]. However, Hsp27 does not appear to enter the nucleus of differentiated striated muscle cells, and although the expression of Hsp27 inhibits apoptotic signaling in both non-muscle cells and undifferentiated muscle stem cells, there is little data to suggest these mechanisms are significant for the protection of mature muscle cells. Instead, numerous studies have indicated that Hsp27 interacts with and protects specific structural proteins in muscle cells subjected to a variety of injury mechanisms. For example, in differentiated striated muscle cells, Hsp27 translocates from a cytosolic localization to a detergent-insoluble fraction and to the apparent Z- and M-lines of sarcomeres in response to a variety of conditions including heat shock [34,35], dilated cardiomyopathy [36] prolonged eccentric exercise [37,38] and ischemia/reperfusion injury [39,40]. Hsp27 has also been shown to protect desmin and troponins I and T from proteolytic degradation in tissues subjected to ischemia/reperfusion injury [22,41]. Finally, Hsp27 also co-localizes with actin filament arrays in injured non-muscle [42,43] and muscle cells [25,44], and overexpression of Hsp27 enhances the resistance of actin filament arrays in these and other cell types to stress-induced disassembly [5,45–47].
The available data regarding distribution patterns of Hsp27 has led to wide acceptance of the view that Hsp27 interacts directly with filamentous actin or components of the actinomyosin contractile system [4,6,48–50]. However, several recent studies have examined the behavior of the Hsp27 homologue, alpha B-crystallin, within mammalian muscle cells [51,52]. In these studies, apparent Z-line localization patterns seen in the resting length myofibrils were shown to be Z-line independent. Instead, alpha B-crystallin was shown to bind to the N2B domain of the giant myofibrillar protein, titin, in vitro and was localized to the putative N2B region in myofibrils subjected to ischemia and varying degrees of mechanical stretch. This interaction alters the mechanical characteristics of titin [53] and may be important for maintenance of titin and sarcomere stability following stress.
Analysis of Hsp27 localization patterns in stretched myocytes has not been previously conducted. In previous studies, we have demonstrated that heat shock induces recruitment of Hsp27 to myofibrils in embryonic zebrafish in a manner that closely mimics the distribution patterns seen in ischemia/reperfusion injury of mammalian muscle tissues [54]. In the present study, we have used this model system to examine the distribution of Hsp27 in resting length and stretched cardiac myocytes of the adult zebrafish under control conditions and after heat shock. Our results confirm that Hsp27 is recruited to zebrafish cardiac myofibrils after heat shock, as it is in stressed mammalian [55] and zebrafish [54] skeletal muscle cells. We also found that stretching alone was insufficient to recruit Hsp27 to myofibrils, and that heat shock-induced recruitment of Hsp27 to the myofibrils is independent of actin filaments. Additionally, Hsp27 did not colocalize with other major sarcomeric components alpha-actinin, desmin or myosin in this model system. Instead, qualitative and quantitative comparison of Hsp27 localization patterns and a marker for titin filaments indicate that Hsp27 is linked to the titin filament system in cardiomyocytes after heat shock. We propose that the interaction of Hsp27 with titin or a titin-associated protein plays a central role in its protection of muscle tissues.
Zebrafish (Danio rerio) were reared and maintained as previously described [56]. Adult zebrafish were heat-shocked in a beaker with 500 mL of fish system water that was gradually raised from 28 °C to 39 °C in a water bath (Isotemp 202, Fisher Scientific, Pittsburgh, PA). Air was continuously bubbled into the water during the treatment. The temperature of system water in the inner beaker was monitored and a 30 min heat shock begun once the temperature reached 39 °C. After treatment, zebrafish were euthanized by rapid immersion in ice water, and hearts excised for further protocols. All protocols for the use of animals in this study were approved by the Washington State University Animal Care and Use Committee and adhered to National Institute of Health standards established by the Guidelines for the Care and Use of Experimental Animals.
Excised hearts were placed in relaxing solution (100 mM KCl,1 mM MgCl2, 10 mM imidazole, 2 mM EGTA, 20 mM 2,3-butanedione monoxime, 5 mM ATP, 1:500 dilution of Protease inhibitor cocktail (Sigma Aldrich P8340)) and dissected into smaller pieces two to three millimeters in diameter. Tissue fragments were incubated in relaxing solution for 5 additional minutes at room temperature. To stretch myofibrils, we adapted a squash technique previously used to examine mitotic chromosomes [57]. Briefly, relaxed tissue was crushed between poly-(tetrafluoroethylene)-coated plastic and a chrome-gelatin subbed coverslip for 30 s using a fingertip. Tissues which adhered to the coverslip were then immediately placed in 4% paraformaldehyde for 30 min at 4 °C followed by processing for immunofluorescence localization of specific proteins. Myofibrils stretched to varying degrees were found randomly distributed throughout such preparations. For the purposes of this study, sarcomeres with lengths similar to those seen in sectioned intact heart tissues shown in Fig. 1 (≤2 μm) were considered "resting length". Where noted, tissues were placed in a lysis buffer (relaxing solution containing 0.1% Triton X-100) for 1 h at 4 °C prior to stretch. For these experiments, control tissues were placed in relaxing solution without detergent for 1 h at 4 °C. A total of 41 hearts were prepared by this stretch protocol for examination under 7 different experimental conditions.
Extraction of F-actin from tissues was performed as described [52]. Briefly, pellets were incubated in 1 mL of extraction (1 M NaSCN in PBS) or control (PBS) solution and vigorously vortexed. After a 15 min incubation at room temperature, samples were centrifuged at 10,000 g for 5 min, and pellets suspended in fresh extraction solution. This procedure was repeated a total of three times for each sample preparation. Final pellets were washed in PBS and suspended in SDS-PAGE sample buffer (10% v/v glycerol, 62.5 mM Tris–HCl, pH 6.8, 2% w/v SDS, 0.01 mg/mL Bromophenol Blue) for Western blot analysis or processed for cryosectioning and immunofluorescence localization of Hsp27. In total, 14 hearts were utilized for Western blot analysis and 4 hearts were used for immunofluorescence localization.
For collection of detergent-insoluble protein, whole hearts were homogenized in a Triton X-100 based lysis solution (20 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.5% Triton X-100, pH 7.3) followed by incubation on ice for 20 min. Pellets were collected by centrifuging samples at 10,000 g for 8 min. Supernatants were discarded and pellets solubilized in SDS-PAGE sample buffer. Protein concentrations were measured using a Bio-Rad Dc Protein Assay Kit. 30 μg/lane of protein (approximately 0.5 hearts/sample) was separated on 4% acrylamide stacking and 12% separating gels, transferred to nitrocellulose membranes (Nitrobind, 0.22 μm, GE Water & Process Technologies) and membranes were subsequently stained with Ponceau S to confirm equal loading of lanes (data not shown). Detection of Hsp27 was performed using an anti-Hsp27 serum described previously [14], or an anti-sarcomeric actin antibody (Sigma Aldrich, clone 5C5), and horseradish peroxidase labeled secondary antibodies. Blots were developed using chemiluminescent detection reagents (Amersham Biosciences Inc.) and images obtained with an Autochemi™ System (UVP Bioimaging Systems, LLC Upland, CA). The integrated optical density (IOD) of bands was measured using NIH ImageJ software (rsbweb.nih.gov/ij/). IOD values were expressed as a normalized percent integrated optical density, where the value obtained for each band is compared to the total IOD for all bands on an individual blot and experimental values were normalized to values obtained from control samples [58]. Each experiment was performed four times.
Tissues shown in Figs. 1 and Fig. 5B were fixed for 30 min in 4% paraformaldehyde following appropriate experimental treatment, rinsed in PBS and frozen in 100% OCT by immersion in liquid nitrogen. 15 μm thick sections were cut using a Reichert–Jung cryotome (Cryocut model 1800) and mounted on chrome-gelatin subbed coverslips. Cryosections were fixed for an additional 5 min on ice. Tissues shown in Figs. 2, ,4B,4B, and and66 were adhered to coverslips as stated in the myofibril stretch protocols section. All samples were permeabilized for 30 min in lysis buffer on ice. Samples were incubated with primary antibodies (1:300 in PBS containing 0.1% Tween 20 (PBS-T) and 10% donor calf serum (DCS)) overnight at 4 °C in a humid chamber. Primary antibodies used were polyclonal anti-Hsp27 serum, anti-desmin (Millipore, MAB3430), anti-alpha-actinin (Sigma Aldrich, clone EA-53), anti-titin, clone T11 (Sigma Aldrich), and anti-MHC F59 (Santa Cruz). The T11 antibody is a specific marker for the A/I boundary of titin filaments [59].
Fluorochrome labeled secondary antibodies were incubated with samples at a concentration of 1:500 in PBS-T with 10% DCS for 2 h at room temperature. F-actin was detected using rhodamine-conjugated phalloidin (Molecular Probes). Coverslips were mounted on slides using Mowiol containing an antifade agent (DABCO, Sigma Chemical Co). Images were acquired using a Zeiss LSM 510M confocal microscope (Carl Zeiss Inc., Thornwood, NY) with a 63×1.4 NA oil immersion objective or a 20×1.2 NA glycerol immersion objective. Post processing of images was conducted using Adobe Photoshop CS2 to enhance contrast. Images contained within the same figure were processed together and identically. A total of 57 hearts were used for 9 immunolocalization protocols.
Fluorescently labeled areas of myofibrils (band) widths and sarcomere lengths were measured using ImageJ version 1.37 (Wayne Rasband, National Institute of Health, Bethesda, MD). Distance measurements were exported to Microsoft Excel, where scatter plots were created for each data set. Linear regression of band width data was performed using Microsoft Excel software. All other statistical comparisons were performed using Minitab version 15. Fitting data to a general linear model was performed to determine statistical significance of linear regression slope comparisons. Analysis of Western blot densitometry was performed using a one-way ANOVA and Tukey's W procedure for data in Fig. 4, and Student's t-tests for data shown in Fig. 5. An alpha of 0.05 was used as a measure of statistical significance in all calculations.
In zebrafish heart tissues fixed under control conditions, the distribution of Hsp27 in cardiomyocytes is largely diffuse (Fig. 1, CN), although a faint striated pattern (inset, solid arrows), can be seen, suggesting that a small fraction of Hsp27 may associate with sarcomeres under control conditions. In contrast, cardiomyocytes obtained from hearts of heat-shocked animal display a dramatic and nearly complete association of Hsp27 with myofibrils (Fig. 1, HS). Regularly spaced, narrow, brightly stained regions (inset, closed arrows) alternate with much more faintly stained areas (inset, open arrows). We have demonstrated similar localization patterns for an EGFP-zfHsp27 fusion protein expressed in zebrafish embryonic skeletal muscle under control conditions and after heat shock [54]. In addition, we have recently demonstrated the specificity of the Hsp27 antiserum used here [14]. Finally, this Hsp27 immunolocalization pattern has also been demonstrated by others examining stressed mammalian cardiac and skeletal muscle cells [34,35,37,38]. Therefore, we conclude that this pattern represents specific localization of zebrafish Hsp27 protein. This pattern is consistent with strong recruitment of Hsp27 to the area of the sarcomere near the Z-line (see Fig. 4B), with some, but lesser, association with M-band structures.
To determine if Hsp27 associates with F-actin, co-localized F-actin and Hsp27 in ventricular myocytes were stretched to varying lengths. Fig. 2 provides representative images showing that Hsp27 (green) and F-actin (red) colocalize in resting length myofibrils (Fig. 2A, top). In stretched myofibrils, F-actin remains as single bands (Fig. 2A, lower panels), and co-staining of these preparations with probes for the Z-line marker alpha-actinin (not shown) revealed that each phalloidin stained band is centered on a single Z-line, as expected. However, increasing stretch resulted in the Hsp27 localization pattern showing increasingly separated doublet bands found progressively outward from the center of phalloidin stained F-actin bands. Finally, in sarcomeres stretched to the longest distances (Fig. 2A, bottom panel), the Hsp27 doublets are spatially distinct from the staining pattern for F-actin. These data are inconsistent with direct interaction between Hsp27 and F-actin.
Next, we assessed the relationship between Hsp27 and a marker for the titin A/I boundary. Fig. 2B is a representative image showing co-localization of Hsp27 and the T11 epitope marking the A/I boundary within a myofibril stretched to an average sarcomere length of 4.4 μm. As shown previously for mammalian muscle cells [60], T11 staining was characterized by doublet bands in all preparations. Myofibrils in these preparations could not be stretched as greatly as those shown in Fig. 2A without loss of defined T11 staining. However, in this and all similar preparations, T11 (red) flanked Hsp27 immunolocalization (green) bands and doublets. Therefore, these data indicate that the site of Hsp27 binding in the sarcomere lies between the Z-line and the A/I boundary recognized by the T11 antibody.
To further assess the relationship between Hsp27, F-actin and titin within cardiomyocytes, we measured doublet band separation for both Hsp27 and T11 staining as well as the width of phalloidin stained F-actin bands in the heart preparations described above. These dimensions were then plotted against the length of associated sarcomeres, and resulting scatter plots (Fig. 3A) were subjected to linear regression. Slopes of the regression lines, which indicate the increase of measured doublet separation (Hsp27) or band length (F-actin) as sarcomere length increased, were 0.8299 for Hsp27 (empty triangle) and 0.1658 for F-actin (solid diamond). Statistical analysis indicated that the slopes for F-actin and Hsp27 were significantly different (p<0.001). These results demonstrate that the measured width of phalloidin stained F-actin bands changes only slightly as sarcomeres are stretched, a finding consistent with the sliding filament model of muscle contraction. In contrast, the separation between Hsp27 doublet bands increases nearly 8 fold greater than the F-actin band lengths over the same sarcomere stretch distances.
We repeated this analysis for data obtained from samples probed with Hsp27 antiserum (Fig. 3B, open triangles) and the T11 antibody, which recognizes the A/I boundary region of titin (solid diamond). The resulting regression lines have slopes of 0.9879 for Hsp27 and 1.0398 for T11 and are not significantly different (p=0.11). The similarity of regression slopes calculated from these data strongly suggests a link between Hsp27 and the titin molecule within the sarcomere. It should be noted that the slope for Hsp27 doublet separation presented here is different than that calculated for Fig. 3A. This is due to our inability to detect T11 staining in myofibrils stretched greater than 6 μm. If the Hsp27 data set shown in Fig. 3A is limited to values less than 6 μm, the calculated slope is not significantly different from that shown in Fig. 3B (data not shown).
It is possible that stretching can alter the association of Hsp27 with myofibrils or revealed Hsp27 binding sites not present under normal physiological conditions. To address these issues, we assessed whether the amounts of Hsp27 present in detergent-insoluble protein fractions were different in resting length and stretched preparations. Fig. 4A shows an anti-Hsp27 Western blot loaded with equal amounts of detergent-insoluble protein per lane. Consistent with results obtained in studies of mammalian muscle tissues and results shown in Fig. 1, the total amount of detergent-insoluble Hsp27 is dramatically greater in heat-shocked zebrafish heart tissue than in control preparations for both resting length (rest) and stretched (str) samples (compare samples labeled CN and HS in Fig. 4A). However, the amount of Hsp27 detected in samples prepared from resting length and stretched tissues were not different within each experimental group (compare samples labeled unstr and str in Fig. 4A). Analysis of percent IOD values for Hsp27 measured from this and 3 additional independent experiments is shown in Fig. 4B revealing a small, but not statistically significant, increase in the amount of detergent-insoluble Hsp27 following stretch with or without heat shock. In contrast, heat shock highly and significantly increased the amount of insoluble Hsp27 in both stretched and unstretched tissues. We conclude that mechanical stretch has only a minor role, if any, in causing redistribution of Hsp27 in this model.
We also considered that alternative Hsp27 binding targets might be revealed or altered by our stretching protocol. To address this issue, we lysed muscle tissues to remove unbound Hsp27 prior to stretching and compared the distribution pattern of Hsp27 and alpha-actinin in these preparations (Fig. 4C, bottom panel) with that seen in myofibrils stretched while intact (Fig. 4C, top panel). However, the localization patterns of Hsp27 (green) in relation to that of the Z-line marker alpha-actinin (red) in these two types of preparations were indistinguishable. Together, data shown in Fig. 4 indicate that the amount and location of Hsp27 recruited to myofibrils is largely independent of stretching, but is instead primarily determined by the heat shock treatment.
To further assess the relationship between actin filaments and the Hsp27 associated with myofibrils, we extracted F-actin from detergent-insoluble pellets obtained from heat-shocked myocardial tissues by incubation with 1 M NaSCN. Fig. 5A shows duplicate Western blots of equal amounts of these samples probed with antibodies detecting Hsp27 and alpha-sarcomeric actin. Percent IOD values measured from this and three other independent experiments (Fig. 5B) show that the amount of Hsp27 in pellets (left panel) does not significantly decrease following NaSCN extraction (p=0.10). However, average percent IOD values for sarcomeric actin (right panel) decreased by nearly 60% in these preparations (p=0.02). Similarly to results published by Golenhofen et al. examining rat Hsp25 [55], our results indicate that NaSCN extracts detergent-insoluble actin from zebrafish myocardial pellets much more efficiently than Hsp27. We also examined the distribution of actin filaments and Hsp27 in detergent-insoluble pellets (Fig. 5C). Results of this analysis show that a total of 45 min of incubation in PBS alone did not noticeably alter the localization pattern of F-actin or Hsp27 associated with myofibrils (compare Fig. 5C, top left with Fig. 1B). In contrast, F-actin, as measured by the presence of rhodamine-labeled phalloidin, was largely removed from pellets by incubation with 1 M NaSCN (Fig. 5C, lower, right). However, Hsp27 remained in pellets after NaSCN extraction and maintained a striated distribution pattern indicative of association with remaining sarcomeric components (Fig. 5C, lower left). The T11 antibody is not suitable for immunoblotting, and we did not conduct Western blot analysis of titin in the present study. However, previous authors have demonstrated titin's resistance to NaSCN extraction at the concentrations used here [52].
Finally, recent studies have shown that Hsp27 can protect a variety of cytoskeletal filament proteins from degradation in stressed myocytes [22,41]. To address whether the association of Hsp27 with myofibrils in heat-shocked myocardium could be correlated with other components of myofibrils, we probed stretched myofibril preparations with Hsp27 antiserum (green, Fig. 6) and antibodies recognizing desmin (red, Fig. 6A) and myosin (red, Fig. 6B). Images shown in Fig. 6A reveal that desmin is primarily detected in stretched myofibrils in single bands and distinct from Hsp27 doublet bands. In addition, as shown in Fig. 6B, myosin localization patterns show no obvious co-localization with Hsp27 in stretched myofibril preparations.
Hsp27/Hspb1 is a small heat shock protein that participates in a variety of cytoprotective mechanisms, including reduction of reactive oxygen species levels [11], anti-apoptotic signaling [12,13,29–33] and the maintenance of cytoskeletal integrity [4]. The mechanisms underlying these functions are not fully understood, and Hsp27 does not appear to exhibit all of these functions in an individual cell type. Expression of Hsp27 has been shown to inhibit cell death and promote contractile function of mammalian cardiomyocytes after ischemia/reperfusion injury [7,8,22,61]. A common feature of the stress response in both muscle and many non-muscle cells of mammals including humans is the translocation of Hsp27 to the cytoskeleton, specifically to actin filament arrays in non-muscle cells and to the Z- and less commonly M-lines for sarcomeres in striated muscle cells. Understanding the interaction between Hsp27 and its cytoskeletal targets is essential to understanding its mechanism of cytoprotection. The present study focuses on further defining the role of Hsp27 in cardiac muscle cells and establishing the zebrafish as a model for determining mechanisms involved in Hsp27-based cardioprotection. We report that Hsp27 is diffusely distributed in the cytoplasm of adult zebrafish cardiomyocytes under control conditions and associates with a single band centered on the Z-line in resting length zebrafish myofibrils after heat shock. This translocation and distribution pattern is identical to that observed in mammalian hearts in response to ischemia/reperfusion injury [36,39,40,44]. Therefore, heat shock of the poikilotherm zebrafish appears to be an appropriate model system to analyze the interaction between Hsp27 and its cytoskeletal target in the myocardium.
Although previous studies have supported the view that Hsp27 associates with actin or actin filaments in stressed cells (see [4] for review), our results demonstrate that the association of zebrafish Hsp27 with myofibrils is independent of actin filaments. In zebrafish cardiac tissues, phalloidin stained actin filaments within myofibrils appeared as a single band centered on each sarcomere's Z-line. Measured widths of these bands were only slightly increased in stretched myofibrils compared to resting length myofibrils, consistent with previously published data from electron micrographs and the sliding filament model of muscle contraction. In contrast, Hsp27 was localized to doublet bands in stretched myofibrils, still centered on the Z-line. The distance of separation between Hsp27 doublet bands was variable and correlated positively with the length of stretched sarcomeres, while the width of phalloidin stained F-actin regions was largely independent of sarcomere length. These data are not consistent with a model in which Hsp27 binds along the length of actin filaments. Additionally, Hsp27 bands were spatially separated from phalloidin stained regions of myofibrils in extremely stretched myofibrils. These data are also inconsistent with binding of Hsp27 to actin filament ends. In contrast, Hsp27 maintained a consistent relationship with T11 stained titin domains, and slopes of regression analysis for both markers, performed on measured Hsp27 and T11 band separation as a function of associated sarcomere length, were indistinguishable. Biochemical extraction of actin filaments from detergent-insoluble fractions of heat-shocked hearts had little effect on either the amount of Hsp27 present in these fractions or the association of Hsp27 with remaining myofibrillar structures. Finally, stretched cardiac myofibrils co-labeled with probes for myosin, alpha-actinin or desmin all failed to reveal an association with Hsp27. Together these data strongly support the hypothesis that Hsp27 does not associate with actin filaments in heat-shocked zebrafish cardiomyocytes, and instead indicate that Hsp27 associates with the titin filament system in muscle cells subjected to an experimental stress.
Interaction between the related small heat shock protein alpha B-crystallin and titin filaments has been previously demonstrated [51,52]. Although several laboratories have documented the expression of a zebrafish alpha B-crystallin orthologue [62], this protein has not been detected in zebrafish cardiac or skeletal muscle. Therefore, it is possible that zebrafish Hsp27 plays the role carried out by alpha B-crystallin in mammalian systems. However, translocation of mammalian Hsp27 to myofibrils in mammalian muscle tissues, which also express endogenous alpha B-crystallin, is well documented [36,39,40,44]. The reported Hsp27 localization pattern in resting length mammalian muscles is indistinguishable from the pattern observed in our studies of resting length zebrafish myofibrils. Sequence comparison of mammalian and zebrafish Hsp27 and alpha B-crystallin proteins also show that zebrafish Hsp27 is much more closely related to mammalian orthologues than alpha B-crystallin in either system [54]. For example, three phosphorylated serines (S15, S78, and S82 in human Hsp27) and a cysteine (C137 in human Hsp27) have previously been shown to play roles in the regulation of mammalian Hsp27 function [63, 64]. All four of these amino acids are conserved in zebrafish Hsp27 but absent in alpha B-crystallin proteins from both systems. Finally, significant interactions between alpha B-crystallin and desmin in cardiomyocytes have been established [52,65]. Here, we show that Hsp27 does not colocalize with desmin after stretch, with Hsp27 being excluded from the desmin localization pattern. We conclude that the association of zebrafish Hsp27 with the titin filament system likely mimics the behavior of mammalian Hsp27 proteins.
Previously proposed mechanisms for Hsp27 cytoprotection in cardiomyocytes have largely focused on the potential of Hsp27 to act as a general protein chaperone for unfolded actin and other muscle proteins either by acting in concert with the high molecular weight heat shock protein Hsp70 (reviewed in [1]) or stabilization of actin filament arrays through lateral or filament end interactions [4,6,48–50]. In addition, Hsp27 expression has been linked to enhanced resistance of myofibrillar proteins troponin [22] and desmin [41] to degradation in injured muscle cells. However, the distribution of Hsp27 in injured muscle cells is often reported to be highly restricted to specific regions of myofibrils. The identification of the binding target for Hsp27 under these conditions may therefore provide important insight into its regulation and function. Here, we report that although the distribution of Hsp27 in resting length myofibrils of heat-shocked zebrafish cardiomyocytes is consistent with data from other systems, its localization as revealed by stretching of myofibrils, is independent of the actinomyosin cytoskeleton, as well as desmin. Instead, the distribution of Hsp27 is consistent with a protein that binds to the I-band region of the titin filament system. Within this region, Hsp27 may bind to either titin itself or a titin-associated protein. In light of these novel data, we briefly consider possible targets for Hsp27 in this model system and implications for Hsp27 function.
Titin integrity is critical to the maintenance of myofibril structure (reviewed in [66]), and a direct interaction of Hsp27 with titin could result in the stabilization of myofibrils in injured myocytes. However, our data do not strongly support this mechanism. The region of titin between the Z-line and A/I boundary that recruits Hsp27 has been well characterized. Within the I-band region of the titin molecule, there are several repeating immunoglobulin-like (Ig) domains, a PEVK domain, and the N2A and N2B alternatively spliced domains. The Ig and PEVK domains are among the first to unfold following stretch and are responsible for much of the passive tension created by the titin molecule in overstretched sarcomeres [67]. These domains could be a target for a general chaperone function of Hsp27 upon stress-induced unfolding. However, the lack of increase in detergent-insoluble Hsp27 following stretch argues against this possibility. The Hsp27 homologue, alpha B-crystallin has also been shown to bind to the N2B domain [51,55]. However, we have observed that Hsp27 binds myofibrils in zebrafish skeletal muscle [54], as well as cardiac muscle, and others have reported similar results for mammalian skeletal muscle. As zebrafish [68] and mammalian [69] skeletal muscle do not express N2B containing titin splice isoforms, the N2B domain is also an unlikely target.
Instead of binding to titin itself, Hsp27 could bind to a titin-associated protein following heat shock. The I-band region of titin is a scaffold for a number of signaling proteins, including DRAL/FHL2 [70] and cardiac ankyrin repeat protein [71]. The interaction of Hsp27 with these proteins could have profound implications for myocytes. Additionally, the N2A domain found in both skeletal and some cardiac splice isoforms of titin is a binding site for p94 [60,72], also known as calpain 3. Although there is no calpain 3 in cardiac muscle, a similar localization pattern has been reported for the ubiquitous calpain 1 [73]. Low level calpain activation is necessary for normal sarcomeric turnover [74], but myocyte injury is often correlated with a massive calcium influx leading to an overactivation of calpain activity [75]. Therefore, Hsp27 may interact with, and perhaps inactivate, calpains following stress similarly to the Hsp27-based inactivation of procaspase 3 cleavage [30]. An inhibition of calpain activity by Hsp27 could explain various data concerning Hsp27-based protection of cytoskeletal components. Also, as calpains participate in necrosis and apoptosis [76,77], an interaction with Hsp27 could explain the apparent anti-necrotic and anti-apoptotic activities of Hsp27 in various cell types. Although further study is needed to resolve these issues, based on the above discussion we feel available data most strongly suggest direct interaction of Hsp27 with regulatory proteins associated with titin filaments, rather than titin itself.
This study demonstrates that Hsp27 translocates to myofibrils of zebrafish cardiomyocytes following heat shock. Localization of Hsp27 in relation to other cytoskeletal proteins revealed that Hsp27 is not associated with actin, actin associated proteins, myosin or desmin. Instead, we demonstrate for the first time that Hsp27 is associated with the titin filament system in heat-shocked cardiomyocytes. Hsp27 translocation is only stimulated following thermal stress as stretch alone is insufficient to recruit Hsp27 to the titin filaments. Further characterization of this interaction may prove essential to determining the cytoprotective mechanisms of Hsp27 within the myocardium of zebrafish and mammalian systems.
We thank Ryan Middleton for expert assistance with zebrafish husbandry and Dr Henk Granzier (University of Arizona) for critical reading of a draft of this manuscript. Support of this work by the National Science Foundation (IOS- 0818993 to EAS) and the NIH Biotechnology Training Program at Washington State University T32-GM008336 (to NRT) is gratefully acknowledged.
PubMed Central Canada is a service of the Canadian Institutes of Health Research (CIHR) working in partnership with the National Research Council's national science library in cooperation with the National Center for Biotechnology Information at the U.S. National Library of Medicine(NCBI/NLM). It includes content provided to the PubMed Central International archive by participating publishers.


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Division of Property information, custody information, and Divorce help provided by an experienced family law and divorce attorney serving the Temecula, Murrieta, and Hemet areas of Riverside County, California.
Dear Famularo & Associates:
Hi. I have a question about custody and visitation of a minor child. I also have a problem concerning division of assets. My boyfriend and I have a child together and we own a home. We are tenants in common. I have paid for everything. I paid for the down payment, supplemental tax bills, and other additions that contribute to the value of the home. My boyfriend has contributed to 1/2 mortgage. He is not willing to accept any offer other than 50% of the home's value.
--D from Murrieta
Dear D:
Since you are unable to file divorce action, you must file two different cases. One is called a "partition action." This must be filed in civil court and will be to divide the family home. In that case, the court can decide what credits each of you may be entitled to for down payments, house payments, etc.
The other case would filed in family court and is a paternity suit. This would be in family court and the court would decide custody, visitation, and child support. The partition action normally takes 1 year. The paternity suit normally takes 3 months.We can handle both. I would suggest you file the paternity suit first, because it is a cheaper and quicker case to prosecute. If he is unwilling to settle the property issues at the same time, then you file the partition action after the paternity suit is completed.
-- Famularo & Associates
If you live in the Temecula, Murrieta, Hemet or Riverside areas of Riverside County, California and have any questions about obtaining property rights, child custody, or if you need divorce information, please feel free to contact our office to set up an appointment with a divorce lawyer at: (951) 816-9543.
For more information, please visit our websites: Family Law Attorney in Temecula, Divorce Attorney in Temecula, Riverside County Family Lawyer


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Monday, 26 September 2011
OOTS: Some Blooming Good News!
5 comments:
How spooky - I think that the weather forecast on the BBC 1 Breakfast Show came from Cricklade this morning ~ I was only half awake at the time :) A greenhouse was featured in which a lot of plants and cuttings are grown on before they go on display.ReplyDelete
Hi Anna - yes, they broadcast the weather forecast from Crocklade yesterday thanks to its BIB success :)ReplyDelete
We learnt loads more on the local news last night: there's a garden behind one of the banks which has been the HQ for the plant growing activities and there's >160 hanging baskets in the town which take a whole day to water - 3x a week!
Or even Cricklade...ReplyDelete
That is a train station..it is beautiful. It is a nice way to start your journey with such beautiful surroundings.ReplyDelete
Michelle - welcome! We had a great day :)ReplyDelete
I love hearing from you and welcome thoughtful conversations :)
Comments aiming to link back and give credence to commercial websites will be composted!


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The Ultimate Wedding Dress Fails! #WEDDINGDRESSFAIL
Whether it's a large or small wedding, the dress is something that all brides want to be perfect. Every bride has an idea of what her dream dress will look like, but for all the brides who find the perfect gown there are brides who are left disappointed and even in tears.
Even if you get the dress there are lots of things that can happen on the road to or even at the wedding. Take a look at these poor brides that had a wedding dress fail.
The grandma fail
This poor grandmother got a bit overenthusiastic and threw her drink over the bride rather than her confetti (big oops!) Although grandma was clearly upset at the time, the bride was able to smile about it (after she'd wiped the drink off her dress) and said it didn't ruin her day. The groom even thanked his wife's grandmother for making the day even more memorable. Thanks to modern technology we can all enjoy this very awkward moment.
The fail of nature
Although incorporating your beloved pet in your wedding might seem adorable, we all know that animals and nature don't always play along with the plan. This poor bride found out that the call of nature isn't easily ignored. When a dog's gotta go, a dog's gotta go!
The thief fail
Imagine you found your dream dress. You've paid for it and have just days until you get to wear it as you walk down the aisle. Then disaster strikes! The dress is stolen, or should we say the minivan you left it in is stolen. That's exactly what happened to this poor bride, and despite her emotional appeals on TV the dress was never seen again. But this story isn't all sad thanks to the kindness of strangers (we admit that we did cry a little watching this).
Badly made dress
While there are so many amazing dressmakers out there, you have to do your research and find a dressmaker who is reputable and has lots of experience. Blogger Elsie got a dress custom made, but it was far from the dress of her dreams. Not only was it a strange shade of yellow, the body and trim were different colors. It was also too long and didn't fit her body, although the seamstress had her measurements! See the dress for yourself...
The online fail
While the internet has given brides a lot more choice when it comes to buying wedding gowns, for all the dream dresses bought online there are brides who have been left in tears by botched orders. This bride didn't receive the dress until the night before the wedding and everything was wrong. Thankfully she was able to get a dress, just four hours before she walked down the aisle!
All fall down
We know the perils of a badly fitting dress, but even if you have a dress that seems to be the perfect fit you need to make sure it's secure. This bride-to-be was certainly left blushing when she had a wardrobe malfunction that was caught on camera. Even more of a reason to make sure you're wearing the right lingerie on your wedding day.


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Breakfast is the most important meal of the day, and now when you book our Breakfast On Us offer, you'll enjoy a complimentary breakfast buffet each morning at B Resort & Spa. Whether you're traveling for business or leisure, we're here to ensure you start your day with the energy needed to B successful.
Offer available for single or double occupancy only.


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In an earlier post, I described some of the "classic" examples that are used in physics classes. I was surprised when, in a lecture on transformers, the teacher didn't mention the role that transformers played in power transmission.
Turns out, I needed to be more patient. Yesterday, the teacher not only described, but actually demonstrated how transformers are used to deliver electricity over long distances. He set up a voltage supply to represent a power station, and a pair of lamps to represent different cities. First, he connected a lamp to the voltage supply, to show that it could light up. Then, he ran wires from the lamp to a pair of 1 kOhm resistors. He explained that if you want to run power over long distances, the resistance of wires becomes a problem. Between the resistors, he wired another lamp - which didn't light up. He increased the voltage so high that the first lamp blew out - to demonstrate that you can't just "up the voltage" and expect things to work out well for everyone. "Oh Noes!" Thought the class, "how will the people of second-lamp-ville get power?" Never fear, for SCIENCE is here!
Wolfi (our fearless teacher) then used transformers to step-up the voltage through the resistors, and then to step-down the voltage to the second lamp. Huzzah! Sweet, delicious electricity flows to the lamp, and they all lived happily ever after. The best part about all this is that the resistors were mounted on stands, so that the wires actually looked like power lines. Wolfi even told me there were covers for the lamps that made them look like houses.
It may not excite anyone else, but I think taking that extra step to make the power lines look like power lines made the demonstration really effective.


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Mission: Strongly rooted in the scientific and research communities and closely aligned with customers and technology partners, Sartorius is dedicated to its philosophy of "Turning science into solutions" every single day.
Founded in 1870 in Goettingen, Germany, Sartorius today is a joint stock company with production facilities, sales subsidiaries and local commercial agencies in more than 110 countries. Sartorius currently employs more than 6,200 people globally, of which approximately 38% are based in Germany. In fiscal 2015, the Sartorius Group earned sales revenue of 1,114.8 million euros. Sartorius has been listed in the TecDax technology index since 2012.
What was important to us then, is still important to us now: close cooperation with our customers and the global scientific community, a forward-thinking outlook, regional roots and a people-focused corporate culture.
As a partner for pharmaceutical and laboratory companies, Sartorius is a global leader in dynamic sectors that will continue to grow for many years to come. Our areas of core expertise are fermentation and filtration technologies, fluid management and purification for the manufacture of biopharmaceuticals, as well as laboratory instruments. Natural scientists, engineers, business managers, you name it – at Sartorius, experts of diverse fields work right along with our partners and customers who are among the best and brightest in their sector.
Expert Career Path
With the Expert Career Path program, Sartorius offers its employees in the Research and Development unit a structured, transparent approach to their career development. Like a manager's career, an expert career covers defined steps up the career ladder, enabling an expert to be promoted several rungs. As a result, experts can focus on the core areas of their work – developing products and driving innovations, without being sidetracked by management tasks.
Sartorius College
At Sartorius, experts can continuously expand their skills and careers, for example, by selecting specific seminars from the comprehensive program of training courses offered by Sartorius College on interpersonal communication, leadership and work techniques or by attending our sales and technical training courses.
Experts who are at the top of their fields in science and technology work at Sartorius, in interdisciplinary and, more often than not, international project teams. At the same time, they benefit from short decision-making paths and the family-style corporate culture at Sartorius. We appreciate individual performance, give individuals considerable freedom in their work and foster an open exchange of experiences and ideas.
Managers and Executives
Sartorius expects its employees to think outside the box, show initiative and be willing to take responsibility. To foster this climate, managers at Sartorius are obligated to create the basic conditions for their teams to perform at their best.
As a partner of the pharmaceutical and laboratory industries, Sartorius is a global leader in the dynamic sectors of the future: staying abreast of evolving technologies and leading changes are part of our daily "bread and butter" business. So this is why we look for managers who will lead change, instead of just following it. Being open-minded to new ideas and approaches is among our most important values.
Sartorius operates at the forefront of science and technology. At our company, products take shape that didn't even exist a few years back. Moreover, we place the highest requirements on our product quality. This is our mission that also serves as a guiding principle for our managers. It is their duty to lead their own unit to achieve top performance.
We look for people with leadership personalities who think beyond department cubicles and country borders and who will actively join us in growing our business in international markets. To help you hone your skills for developing your personal career, you can choose the right program from the comprehensive offering of further training courses held at Sartorius College.
You have successfully completed your studies or vocational training and now want to enter the working world? Start your career with a company whose products and technologies are among the best in a growing and innovative industry.
At Sartorius, you will be working for a technology group that is represented in over 110 countries. Openness to new ideas and the creativity to make them a reality are the cornerstones of our way of doing business. Thanks to flat hierarchies and short decision-making channels, young professionals at Sartorius can make a difference right from the start.
Regardless of whether you already have a clear idea of your career path or simply want to get a taste of what's out there – Sartorius puts a world of development opportunities at your feet.
Internships for University Students
Are you studying engineering, natural sciences, business or information systems management and looking for an interesting internship? Sartorius can offer you interesting internships in all company departments, such as in Research & Development, Quality Management, Sales, Marketing, Corporate Communications, HR or IT. Even as an intern, we integrate you into ongoing projects and our day-to-day operations.
Regardless of whether you seek a pre- and/or basic internship, compulsory internship or practical semester – we are as flexible as you are when it comes to internship dates: Anything from 6 weeks to 6 months is possible. Remuneration is based on the duration of the internship and the amount of study you have completed. You can read more about the specific criteria and requirements for our internships in our Frequently Asked Questions section or in the job descriptions for each of our vacancies.
Student Traineeships
Are you looking to gain practical experience, but don't want to take time off from your studies? If that's the case, you can work for us as a long-term Student trainee alongside your studies and reap double the benefits: You gain key professional experience while earning some money on the side. The reduced number of weekly working hours (usually 10 to 20 a week) let you continue to concentrate on your degree while working at Sartorius.
Interested? Then take a quick look at our Online Job Portal to see whether there's something offered that fits your needs. If the right position is not available at the moment, order our job subscription and you will always be informed immediately about new job offers that might be of interest to you. Perhaps our paths will cross in the future. For further general information on internships and student traineeships with Sartorius and on the application process, have a look at our FAQs.
In any event: Good luck with the rest of your studies!
With ideas, expertise and a passion to excel, our employees contribute immensely to the success of our company. We empower them to use their skills to their fullest potential. We offer motivating work conditions, comprehensive training seminars, and flextime work schedules. Innovative and dynamic, international and family-style, with strong values and roots: working at Sartorius is something really special.
Sartorius offers its employees all the benefits of a large group: the enjoyment of working in an international environment, a comprehensive and progressive human resources development policy, attractive compensation and, last but not least, the flexibility to enable them to set their work hours to suit their lifestyles. At the same time, they enjoy all the benefits of a medium-sized company: short decision-making chains and fast lines of communication.
An Inspirational Working Environment
We offer you a secure and pleasant environment so that you can fully concentrate on your tasks, maximize your full potential and come up with new, creative ideas. Sartorius wants employees who show initiative and are willing to take on responsibility. In return, they can expect a lot from Sartorius.
Our employees receive bonuses in accordance with local standards. In addition, Sartorius offers company paid contributions to health insurance and retirement plans.
Multifaceted Human Resources Development
As a supplier for pharma and biotech companies, Sartorius is a worldwide leader in growth markets. The dynamics of our industries are paving ever newer ways for our employees to evolve. We continuously invest in the further development of our human resources. Indeed, we require competent and qualified employees who would like to grow alongside us.Human resources development is not a standard process for us. We support our employees with custom-tailored measures meant to help them achieve their career goals. If they wish to do so, our staff can even receive training beyond their actual work area and perhaps even discover talents they didn't realize they had. By taking part in job rotations, where employees transfer to other corporate locations, sometimes even international ones, "Sartorians" can expand their personal and professional horizons. Additionally, we offer personalized developmental assessments so that individuals can expand their competencies and hone their strengths Our employees can choose from numerous training courses, seminars, and language courses that prepare them for the next higher expert or management levels. Many of them are held at the Sartorius College in Goettingen.
Health Management & Occupational Safety
A healthy company needs healthy employees. Company-wide health management is not an obligation, but rather a matter of heart for us. Depending on site locations, we offer a range of comprehensive health screening benefits, medical check-ups, consulting services and concrete occupational safety measures. We take care of everything to ensure healthy working conditions, as safety and health have top priority at Sartorius.
As an industrial corporation, occupational safety is a major focal point at Sartorius. We are continuously improving technical and organizational working conditions to keep the number of work-related medical conditions, health hazards and accident risks as low as possible. We achieve this through technical improvements and regular training courses.
Company Sports
In several countries, Sartorius organizes company sports events to encourage healthy lifestyles. By taking part in one of the numerous company sports groups, colleagues also get a "sporting chance" to get to know each other and stay fit together. Whether playing soccer, sailing or jogging in a group, the main focus is the enjoyment of exercising together.
The basis of your career is your professional expertise. You enjoy working with professionalism, constantly learning new things and thinking outside the box. Then you will fit in well at Sartorius. As a supplier and partner of pharmaceutical and biotech companies, we are a global leader in highly dynamic sectors that will continue to grow for many years to come. This means that the demand for new technologies will steadily increase in the future as well. To meet such growing requirements, we are looking for people who would like to shape new developments. At Sartorius you will be working at the cutting edge of science and technology, on products that didn't even exist a few years back – and with colleagues, partners and customers who are among the best in their field.
Sartorius earns more than 85% of its sales revenue outside Germany and is represented by its local manufacturing sites and sales companies based across the globe. Over the next few years, we will aim to fast-track our growth primarily in the USA and in Asia, above all through our own strengths, yet also by targeted acquisitions and alliances. This is why that for our international projects, we are looking for people who will proactively strive along with us to develop these growth markets. The sheer variety of our prospects and open exchange are the sources of our progress and change.
Not interested (anymore) in working at a little job in a big company? If you do not like being just one of the nondescript masses who are responsible for taking care of small details, then Sartorius is the right place for you. We expect you to think on your own, take the initiative and be willing to assume responsibility. Rigid hierarchies and long-drawn-out decision-making processes are not our thing at Sartorius. Instead, we see and appreciate individual performance and give each employee lots of space to develop. With us, you can realize your full potential to promote our company's growth and your personal career.
Founded in 1870 as a spin-off of the University of Goettingen in Germany, Sartorius offers an attractive combination of tradition and innovation, and of regional roots and global flair. At many of our international sites, we have been a presence for decades. What's more, Sartorians are united across the world by sharing our three corporate values: sustainability, openness and enjoyment. To enable you to "take root" with us, we will offer you not only a family-oriented corporate culture, but also realistic, individualized employment opportunities. When you work with us, you'll have the flexibility you need to successfully master the challenge of balancing your career and family.
Sartorius has evolved from a small workshop for mechanical instruments into an international group of high-tech companies with more than 6,200 employees. Yet our multinational corporation has retained the essence of what defines us as a group: close cooperation with our customers and alliance partners, our cosmopolitan outlook, regional roots and a people-focused corporate culture.
Sartorius works for sectors that are required to meet high quality and safety standards. Close relationships with customers as our partners are therefore the foundation of our business. Such bonds built upon trust are more important to us than short-term profits. By collaborating closely with scientific institutes and universities, Sartorius remains at the forefront of the latest developments and, as a technology leader, sets the standards in many market segments. In fact, ever since it was founded, our company has always fostered open exchange with the scientific community, helping it to move forward.
Long-term relationships, enjoyment shared while working together, exchange of ideas as equals – all this is also part of everyday work inside Sartorius. It is no surprise that the strong identification of Sartorians with their company is a common thread woven throughout its history. In Germany, for instance employees stay with us around 14 years on average.
In autumn 2013, Sartorius conducted its first Group-wide employee survey. Both the response rate and overall Evaluation were clearly above those of comparable studies, underscoring the high engagement of Sartorius staff. We plan to repeat the employee survey exercise at regular intervals in future to enable us to identify changes over time and investigate their significance.
I have been working at Sartorius full-time (More than 10 years)
Growing company, opportunity for training, stability, opportunity for interaction with different business areas and global colleagues, good benefits, market leader, global company, other career opportunities, bonuses
Some managers do not take any interest in your career - you're completely on your own no matter how many contributions you've made, size hinders communication, German centric, lack of sufficient knowledgeable resources means you will be covering for others or doing their job, office is open plan and distracting when the usual socializers can't keep a lid on it, Market based compensation can prevent any further salary increases if you've been there awhile and have reached the top of the range.
Advice to Management
Talk to the people below Director and Manager level.
I applied online. I interviewed at Sartorius (Bohemia, NY) in May 2017.
The process is a little long but very thorough and pleasant. The company seems very professional and organized. I am still awaiting their decision but I feel I am being considered as a serious candidate.
Interview Questions
Let us know if we're missing any workplace or industry recognition – Add Awards


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Rod is a Principal with Acrelic Group. Prior to Acrelic, Rod was a board member of SCT Corp who helped orchestrate its growth and acquisition by Campus Management Corporation. From January 1998 until his retirement in May 2001, Rod Everhart served as President of SCT Global Education Solutions. Mr. Everhart and the executive team established the vision and the growth strategies for SCT's largest division. This was his second affiliation with SCT; from 1985 to 1989, he was Vice President, Finance & Administration, Treasurer, and Chief Financial Officer for SCT.
From 1989 to 1995, Mr. Everhart served at LexisNexis (then Mead Data Central, Inc.), first as Vice President, Financial Resources & Administration, and then as President beginning in 1992.
Following LexisNexis' divestiture to Reed-Elsevier plc, he joined Bellcore (Bell Communications Research, Inc., now Telcordia Technologies) as Senior Vice President and Chief Financial Officer. He also directed the company's corporate communications and human resources. Prior to 1985, Mr. Everhart had a 19-year career in financial management with General Electric Company.
Rod currently serves as a board member of Campus Management Corp.
He holds a BS in Management from the University of Illinois, Champaign-Urbana, and is a graduate of General Electric's Financial Management Program and other advanced courses.
E-mail: email@example.com


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Friend Frame – Personalised Gifts
Friend Frame - Personalised Gifts
This frame is a wonderful way to tell a friend how much they really mean to you!
Just add a personal message (in the box below "Personalise your product") and it will be displayed in the bottom right hand corner. i.e. "Happy Birthday, Love Andrew xxx".
Your artwork will be sent via email for your approval before it is sent to print.
All frames are printed on high quality cartridge paper, tied in a white silk ribbon, gift wrapped with Dollie Graphics seal of approval. Dollie Graphics also offers FREE local delivery (within H&F).
To add your own words please add them in the 'personalise your product' box. And please select the frame colour from the drop down. If you would like to change the colour scheme this can also be done, please just ask.
Frame size is 32cm x 42cm and design is A4.
More personalised gifts available:


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Many patients ask, "After you remove my cataracts, will they come back?" The short answer is no, but a patient's vision can get cloudy again, even after perfect cataract surgery. Here's the explanation, courtesy of Dr. Zack Burkhart... At the time of cataract surgery, the surgeon removes the patient's cloudy lens from the lens capsule.…Read more
The Golden Rule at Focal Point Vision
If you are reading this Blog you are most likely on the quest to find clearer vision. Be it cataract surgery, LASIK, Corneal Transplant or possibly Crosslinking for Keratoconus. You've searched online, asked your family and friends and exhausted all avenues you can think of to find the eye care provider to give you the…Read more


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Error Mounting
In the grub menu select ubuntu and boot it.After the ubuntu booted up,now open the ntfs hard drive partition,it will open. Check to see if you have a mount point (folder for mounting your partition in) for your Windows partition in the folder /media using this command: ls /media If you don't Wenn du bei YouTube angemeldet bist, kannst du dieses Video zu einer Playlist hinzufügen. Please can anyone help me on this? check over here
If you dual boot and need access to that data in Ubuntu, the decrease in Windows startup time is worth the utility of having access to your disks. Thanks .. Anmelden 25 Wird geladen... I can finally access on it under my Manjaro Linux. read review
Error Mounting /dev/sdb1 At /media/
Wähle deine Sprache aus. share|improve this answer answered Sep 1 at 17:15 Philipp Claßen 2412412 add a comment| protected by Community♦ Oct 24 '13 at 5:27 Thank you for your interest in this question. What version of Windows do you use? –yanglifu90 Aug 26 '12 at 7:22 add a comment| 18 Answers 18 active oldest votes up vote 200 down vote accepted A bug has
Because it has attracted low-quality or spam answers that had to be removed, posting an answer now requires 10 reputation on this site (the association bonus does not count). Hinzufügen Möchtest du dieses Video später noch einmal ansehen? Thanks! Error Mounting /dev/sdb1 Reply JohnC says September 29, 2014 at 3:59 am I agree with you.
For this follow the steps as below 1. Error Mounting /dev/sda2 Would you like to answer one of these unanswered questions instead? Any other suggestions? Reply Andreas Roy says February 4, 2014 at 3:30 am I have a similar problem to that of some people here.
Schließen Weitere Informationen View this message in English Du siehst YouTube auf Deutsch. Error Mounting /system Wird verarbeitet... Failed to mount '/dev/sda5': Operation not permitted The NTFS partition is in an unsafe state. Software center - APT way to get Adobe Flash Player latest version for Linux not working.
Error Mounting /dev/sda2
After searching the internet for the problem, I think the problem is caused by hybrid shutdown (logoff+hibernation).
DISTRO: Xubuntu 14.04-64bit --- Code-tags --- Boot-Repair --- Grub2 wiki & Grub2 Basics --- RootSudo Adv Reply Page 1 of 2 12 Last Jump to page: Quick Navigation General Help Error Mounting /dev/sdb1 At /media/ Cheers :-) Reply Abhishek Prakash says October 9, 2015 at 12:59 pm Welcome Bob Reply Rusel Cierto Trinidad says September 25, 2015 at 5:30 pm Please resume and shutdwon Windows fully Error Mounting Mount Unknown Filesystem Type 'exfat' Anmelden Statistik 64.996 Aufrufe 377 Dieses Video gefällt dir?
You can change this preference below. check my blog It should be 'Windows something' instead of 'Ubuntu'. If those answers do not fully address your question, please ask a new question. 3 "Windows is hibernated, refused to mount." Unless Windows was completely shut down it's in a Part of the metadata about the state of all mounted partitions at the time of But in fast start up, Windows 8 saves some system information such as caching the registry Error Mounting /sdcard
Source: Arch Wiki (NTFS-3G: Metadata kept in Windows cache, refused to mount): The problem is due to a feature introduced in Windows 8 called "fast startup". Wenn du bei YouTube angemeldet bist, kannst du dieses Video zu einer Playlist hinzufügen. I can only mount RO. this content I followed the instruction of section 2.6 of the following link: https://doc.ubuntu-fr.org/gnome-disk-utility#monter_une_partition_automatiquement_au_demarrage It's in french, sorry.
Last Digit of Multiplications Can my party use dead fire beetles as shields? Error Mounting Location Volume Doesn't Implement Mount Melde dich an, um dieses Video zur Playlist "Später ansehen" hinzuzufügen. This is despite me disabling fast boot prior to that.
What they have done is make it so that when you turn off your computer it really goes into hibernation for a quicker boot when you switch it on again.
Wird geladen... Can you mark your thread as solved from the Thread Tools menu at the top, please. no need to use force –Matthew Sainsbury Aug 1 '14 at 17:06 @Matt I tried shutdown /s /t 0. Error Mounting Lockproto Lock_dlm Reply Trackbacks Instalação do Windows 10 e Ubuntu 14.04 com UEFI | Lcomlinux says: June 6, 2016 at 7:37 pm […] você precisar de mais dicas, siga este tutorial imagem para
You have only one operating system and ie.e Ubuntu, so you should have access to all the hard drive. Veröffentlicht am 29.01.2015can't mount or even boot my windows disk after I installed ubuntu.1) press ctrl+Alt+t and type following command 2) sudo ntfsfix /dev/sda33) press enter 4) Type your password 5) Schließen Ja, ich möchte sie behalten Rückgängig machen Schließen Dieses Video ist nicht verfügbar. have a peek at these guys Wird verarbeitet...
Melde dich bei YouTube an, damit dein Feedback gezählt wird. If I press Mount volume I get this error: Error mounting volume An error occured while performing an operation on "NewVolume"(Partition 1 of ATA ST375084AS): The operation has failed details: Error Because i install ubuntu replacing on window8.


text: News & Comment Computer Sales to U.S.S.R.: Critics Look for Quid Pro Quos + See all authors and affiliations Science 08 Feb 1974:Vol. 183, Issue 4124, pp. 499-501DOI: 10.1126/science.183.4124.499 Nicholas WadeFind this author on Google Scholar Find this author on PubMed Search for this author on this site Article Info & Metrics eLetters PDF This is a PDF-only article. The first page of the PDF of this article appears below.


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Dog Veterinary
Ask a Dog Vet and Get Answers to Your Dog Health Questions
I'm sorry to hear of this with Buddy. Losing coordination (ataxia/"drunken sailor"?) and his way (disorientation) indicates encephalopathy (brain disorder). Both intracranial (within the skull) encephalopathies such as brain tumor in a 9 year old and extracranial (outside the skull) encephalopathies such as a poorly functioning liver that's intoxicating the brain need to be considered. The "bright red eye" has many different etiologies and must be examined directly by Buddy's vet in order to clarify what it represents. It may or may not be related to his other symptoms. Buddy isn't a patient who can be managed at home at this time. Please have him attended to by his vet at your earliest convenience.
Please respond with further questions or concerns if you wish.
My condolences for your loss of Buddy. I appreciate your taking the time to let me know.
You may receive an inappropriate follow-up from the site ostensibly sent by me. It wasn't and I apologize in advance should you receive it.


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B. Duke Lechtman
Integrated Wealth Management
1 Harding Rd, Suite 100
Red Bank, NJ 07701
Tel: 732-510-1600
Direct Line: 732-510-1611
Main Office:
Summit Financial Resources, Inc.
4 Campus Drive, 2nd Floor
Parsippany, NJ 07054
973-285-3600Email: firstname.lastname@example.com
Duke and his wife Susan have lived in Morristown since 1996. Prior to that they resided in Short Hills for 27 years where Duke was among the founders of the Millburn Soccer Associates. Whenever possible, they travel to their country home in the Berkshires with its many cultural activities. In addition, they enjoy tennis, golf and hiking. They have two children and four outstanding grandchildren.
- Wharton School of Business, University of Pennsylvania
- BS Economics
- Family Wealth Planning
- Asset Protection
- Retirement Planning
- Estate/Wealth Distribution Planning
- Investment Planning
Business Experience
- Integrated Wealth Management-Financial Planning (2002-Present)
- Rothstein-Lechtman Associates-Insurance Advisor (1993-2002)
- Founder-SLR Mgt Corp.-Real Estate Management (1985-Present)
- Founder-Income Growth Associates-Registered Investment Advisor (1982-1987)
- Salomon Brothers-Vice President (1962-1980)


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Apr 142015
The big Native Plant Sale (formerly held on 3601 Valley Drive) is renamed the "Northern Alexandria Native Plant Sale" and will be held Saturday, April 25, from 9 a.m. to 2 p.m. This is the 24th occurrence of this twice-a-year, non-profit, community plant sale. Fifteen vendors from four states will be hosted.
Please note that the event has been moved to The Church of St. Clement at 1701 N. Quaker Lane, Alexandria, VA 22302. (This new location is still near Shirlington and is about a half-mile from Parkfairfax.)
The Church of St. Clement is inside I-495 Beltway, near Shirlington & Parkfairfax. From I-395, exit Shirlington/Quaker onto Quaker. After the first light on Quaker, take the next left on Crestwood. Find your parking space on Crestwood or nearby. The sale will be visible on the right at Quaker & Oakcrest (at 1701 N. Quaker Lane).
Please pass this email along to any interested friends. This native plant sale depends on word-of-mouth support. If you would like to post a flyer at work or your local coffee shop, download an updated flyer for the sale from the website at http://home.earthlink.net/~
Looking for more fun things to do? Check our Playdate calendar or volunteer to host a playdate near you!Thank you for being here! People like you make our group go! The Joy Troupe NOVA Moms get the very best Mom News in their inboxes every week! Our members get priority invitations to our awesome FREE family events and group discounts, too. We have so much fun, and we are looking forward to getting to know you and your family! (Membership is always free!) As a bonus, you'll also get to download our 2009 cookbook e-version FOR FREE!
April 14, 2015 Alexandria Playgroup, Northern VA Community Events Add comments


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Welcome to the OLISSA website!
OLISSA is the student organization for the University of Oklahoma School of Library and Information Studies.
Our mission is to bring library students together with one another, faculty, and library and knowledge management professionals. The organization's primary purpose is to represent and serve the SLIS student body. To find out more, see About OLISSA or check out our Facebook page! Just sign into your Facebook account and search for OLISSA.
Upcoming Events
- Mar. 10-11, 2010:
- Dr. Loriene Roy's Presentation
- Wed. nights:
- Comps Study Sessions
- Mar. 26, 2010:
- Comprehensive Exam
- Mar. 27, 2010:
- SLISebration
- Apr. 19-21, 2010:
- OLA Annual Conference
2010-2011 OLISSA Officers
- President:
- Rumela Bose
- Vice President:
- Yao Chen, Vice-President
- Secretary:
- Shae Mitine, Secretary
- Treasurer:
- Julia Robinson, Treasurer
Amanda Hegge, Co-Tresasurer
- Tulsa Liaison:
- Deborah L. Moreau (Emrys), Tulsa Vice President
Remember these upcoming events:
- Dr. Loriene Roy, SLIS Directorship Candidate, will give a presentation and meet with students in Norman on Wednesday, March 10, 2010, 3:30 - 4:15 pm, in Bizzell, Room 100, and in Tulsa on Thursday, March 11, 2010, 2:00 – 2:45 pm at the Schusterman campus, Room 3J23.
- SLISebration will be held Saturday, March 27th at the Oklahoma Memorial Union.
- A retirement reception in honor of Dr. June Lester will be held at the Oklahoma Library Association Conference on Monday, April 19, 2010, at 5:30 pm. Students and collegues are encouraged to attend. Attendees do not have to register for the OLA Conference to attend this event.
- Continue to look here for future announcements!
Budgetary Matters
OLISSA is a recognized student organization at the University of Oklahoma and receives a budget through UOSA. We use these funds for:
- workshops, colloquia, and panel discussions of interest to the student body
- sponsoring attendance at regional and national conferences
We welcome contributions from all OLISSA members to help keep our site up-to-date and informative. If you have questions or comments regarding this website, please contact Chrissy Shackle.
Recent Events
- Mar. 1-2, 2010:
- Dr. Cecelia Brown's Presentation
- February 23:
- Dr. Wallace Koehler's Presentation
- February 9:
- OLISSA Officers' Meeting
- February 3:
- SLIS Student Advisory Council Meeting
- December 3:
- Book Sale
- October 5:
- OLISSA Colloquia
OLISSA Committees
OLISSA has committees that are focused on improving the SLIS experience.
- Administration
- Academic Programming
- Projects
- Student Support
- Professional Development
- Mentor Study Group


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Pharmacy Questions? Ask a Pharmacist Online.
Hi, and thanks for your question. I'm DrMike, a pharmaccist with over 20 years experience. -Glad to help you today!
It is possible, yes, for the Dramamine to have caused such a reaction. It's unlikely it was an intereraction between the beer and the Dramamine, but more likely a reaction to the Dramamine.
It would be OK, yes, to take the Xanax... it's a smaller dose and there would be little chance for any significant interaction with the Dramamine or the beers - just increased drowsiness, but it may well help with your situation currently.
Does this address your question?I'm happy to assist if you have further concerns..
(Please Accept and Rate when you are satisfied - I'm glad to be of assistance.) -DrMike
Hi, Brian...I'm just checking in with you after you asked your question last night. Did the agitation subside at all, and were you able to get some sleep?I don't know if you had conferences today, but I know how important sleep is!Let me know if you need further assistance with anything - DrMike(I believe this should address your original concerns? Kindly Accept and Rate my services with you. If you do need additional information simply Reply, and I will be happy to help with any follow up questions. I do wish you all the best...)


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History and Trivia Edit
With hopes of finding info about her parents in the Forbidden Library, Jacqueline brought the Jack O'Lantern Circus to the capital. As she walked with a girl from her troupe, the girl's crimson hair billowed out suddenly. A sea of dragons flew overhead.
Unit Data Edit


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No products
> Hundreds of options to choose from
> View our huge collection
> Store Hours and Locations
We are Canadian Paintball®. Badlands Paintball has been passionately involved with paintball since 1988. Badlands started out with a single location in 1988 and has grown into a nationwide retailer with five Canadian store locations and a distribution warehouse in Toronto.
Over the years we have learned a few things when it comes to the game of paintball. Whether you are just getting started or an avid paintball player, Badlands Paintball stocks paintball guns, paintball masks, paintball hoppers and paintball gear for every type of player.
Our knowledgeable staff will be happy to assist you by email, phone or live chat. We love to talk paintball supplies and would enjoy answering your questions - it is what we do.
Email:[email protected]
Phone: (800)-717-5314
Live Chat: Start Chat >
If you would like to play the game of paintball, there are a few primary paintball supplies you will need. This includes a paintball gun, paintball mask, paintball hopper, paintball air tank and paintballs. Badlands stocks a variety of these items in multiple types,
The paintball gun is a core piece of equipment in the game of paintball. There are many brands and styles available. When you first start out, depending on your budget, you can get an entry level blowback paintball gun at an affordable price. Most entry level guns can be enhanced by adding new paintball gun upgrades. If you want some serious firepower, contact us on the Live Chat to explore the best available options.
Learn More about Paintball Guns >
The paintball mask is a required piece of paintball equipment and for safety reasons, you cannot play paintball without them. Paintball playing facilities require the use of proper ASTM* approved paintball masks. Most paintball masks come in one universal size with adjustable straps. Not all goggles are built the same and they vary by how much comfort,
Learn more about Paintball Masks >
*Your safety is important to us, we stock the paintball masks that meet ASTM guidelines for quality and safety. Shop with confidence when choosing your paintball mask.
The paintball hopper holds extra paintballs before they are fired. Most paintball hoppers have a 200 round capacity. There is a full variety of paintball hoppers ranging from basic gravity fed hoppers to force fed battery operated paintball hoppers. Most players begin with
Learn more about Paintball Hoppers >
The paintball air tank stores gas that is used to propel the paintballs out of the paintball gun. There are two main types of gas, either CO2 or compressed
Learn more about Paintball Air Tanks >
In order to play paintball, it is a given that you will need paintballs to shoot at the opposing team. Despite the name "Paintballs", they are not actually filled with paint. They contain a mixture of ingredients that are easy to clean off once a player is hit. Paintballs can vary in quality based on a few key factors which include Shape, Fill Color, Brittleness, Fill Density and Age.
It is a
All of our stores offer a wide selection of airsoft guns and equipment, making us the only Canadian airsoft store chain with national coverage. Toronto airsoft players can visit our Toronto Megastore location, which offers a huge selection of airsoft guns and gear to choose from, and expert staff to help you make the best
Our knowledgeable staff will be happy to assist you by email, phone or live chat. We love to talk airsoft and would enjoy answering your questions - it is what we do.
Email:[email protected]
Phone: (800)-717-5314
Live Chat: Start Chat >
If you would like to buy airsoft gear, there are a few primary products you will need. These include a primary airsoft gun, airsoft bbs, and airsoft goggles (eye protection). Depending on which airsoft gun you choose, you may need an airsoft battery & charger, green gas, or CO2 cartridges. We recommend adding some spare magazines for your airsoft gun, and an airsoft gun bag!
The airsoft gun is the core component to the game of airsoft. When choosing an airsoft gun, there are a variety of options, including guns made to one-to-one specifications of real-steel guns. You will even find some models available from your
Learn more about Airsoft Guns >
In order to play airsoft, or to shoot targets, you will need airsoft bbs. There are different brands, weights,
Learn more about Airsoft BBs >
Airsoft goggles are a required piece of equipment for safety reasons - you cannot, and should not, play airsoft without them. Airsoft parks and playing facilities require the use of an ANSI approved lens. Most airsoft goggles come in a universal size with adjustable straps. Not all airsoft goggles are built the same, and they vary by quality of vision, comfort, style, protective coverage, and price. We stock a variety of options.
Learn more about Airsoft Goggles >
*Your safety is important to us, we stock airsoft goggles that meet ANSI guidelines for quality and safety. Shop with confidence when choosing your airsoft eye protection.
**Paintball goggles are ASTM certified (rated higher than ANSI) and are approved for airsoft use.
We recommend getting an airsoft gun bag. Gun bags can also be considered a safety device by keeping your airsoft gun out of sight during transport. Reputable airsoft stores and shops, outdoor parks, and indoor playing facilities require the use of gun bags. Beyond safety, the gun bags offer padding and thick rugged materials to help keep your airsoft equipment from getting damaged.
Learn more about Airsoft Gun Bags >
AEG (automatic electric guns) require the use of a battery to power the motor. Airsoft batteries come in a variety of configurations, materials, connection types, voltages, and power (mAh). With all of the options available, it can be confusing to choose the right airsoft battery for your gun. We have a full section on our website with detailed information to help you choose the right airsoft battery for your gun.
Learn more about Airsoft Batteries >
Carrying spare airsoft magazines will allow you to stay engaged in the game
Learn more about Airsoft Magazines >
If you are in the GTA - come visit our Toronto Airsoft Megastore. We have everything you need to play airsoft, and expert staff, who play airsoft, to assist you with any questions you may have.


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$ 20.00
Are you a cat lady? Do you also love Christmas? Look no further for the shirt you're going to wear to the holiday parties this year! This design combines the ugliness of an ugly Christmas sweater with the best animal —cats, duh! Meowy Catsmas!
♥ Exceptionally Soft Poly-Viscose Blend
♥ Our eco-friendly ink is digitally printed into our shirt fibers for a soft feel that will never crack or peel.
♥ Our women's racerback tanks are fitted in the chest and flow away from the body.
Please refer to our FAQ page for shipping and sizing info.


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At Orner Law, LLC, we are committed to providing our clients with the most up-to-date information possible. Below are several informative resources related to business litigation, contract litigation and also non-compete agreements:
Business Litigation Resources
- Business Law (find information on small business regulations)
- Business Formation
- Small Business Law
- What is Business Law/Commercial Law?
- Guide to Commercial Law
Contract Litigation
- What is a Contract?
- What is Contract Law?
- Breach of Contract Explained
- Copyright Infringement Explained
- Intellectual Property Explained
- The Contracts Dispute Act
Non-Compete Agreements
- Non-Compete Clause Explained
- What is an Employee Non-Compete Agreement?
- Understanding Non-Compete Agreements
The resources listed above are meant to provide people with general information related to business law. However, if you have questions or need information that is not covered in the aforementioned resources, do not hesitate to set up a free initial consultation with the Boca Raton business litigation lawyers at Orner Law, LLC. At Orner Law, LLC, our team has 35 years of combined experience handling business litigation matters in South Florida and neighboring cities. When it comes to business law, few other law firms match our skill set, years of service and expertise. We are dependable, accessible attorneys that are committed to our clients and their needs.
Experienced South Florida Business Law Attorneys
With offices in Boca Raton and Fort Lauderdale, Orner Law, LLC serves clients throughout South Florida.
If you need assistance with a business litigation matter in South Florida, contact the Florida business litigation attorneys at Orner Law, LLC. Our law firm has been dealing with complicated business law matters for numerous years. We are loyal to our clients and committed to protecting their best interests and confidentiality.


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About the Company
Foreign Trade Agent
Customs Brokerage Activity
Freight Forwarding Services
Legal Support
Consulting on FEA
Customs Bonded Warehouse
Рlacing Goods at the Temporary Warehouse (TW)
Legal Entities
Physical Entities
Emergency Service
Customs Clearance
Risks Associated With Customs Clearance (Processing)
During customs clearance, coming of goods with risk profiles, in the framework of the SCSU automised system of risk analysis and management, with the further strengthening of customs control.
During exporting, coming of goods with risk criteria, in accordance with the Joint Order of the State Tax Administration of Ukraine and SCSU dated July 12, 2004 N 512/387 (The State Control on Performing Exporting Operations with Certain Kinds of Goods).
Application to a FEA company of the special sunctions of the Ministry of Economy of Ukraine: imposing a penalty, temporary embargo, individual licensing (Article 37 of the Law of Ukraine On Foreign Economic Activity dated April 16, 1991 N 959-XII).
Refusal of a Customs Authority to accept a contract and (or) documents for customs clearance, due to their incomplience and/or violation of requirements of legal regulatory acts.
Embargo by Customs Authorities and/or other State Authorities of importing goods into Ukraine or exporting goods from Ukraine (Article 196 of the Customs Code of Ukraine).
Delay in customs processing, with additional expenses for storage of goods at Temporary Storages, Customs Warehouses, re-processing of documents, division of a commodity lot for sepaprate goods in accordance to their types and (or) articles, etc.
Examination of goods at Customs, with additional expenses for loading-unloading of goods, restoration of marketable conditions of broached pack, etc.
Costs for examination of goods.
Changing of a code of a commodity in accordance with the UCC FEA declared by the FEA entity, by Customs, that causes increasing of obligatory customs fees and duties and/or obtaining additional permissions from State Authorities.
Correction of a declared customs value of goods by the Customs that that causes increasing of obligatory customs fees and duties.
Requesting additional documents from the FEA entity by the Customs.
Refusal of the Customs to provide a privileged regime to the FEA entity.
Refusal of the Customs to provide preferences on the customs duty and VAT to the FEA entity.
Suspension of customs clearance of goods on the basis of data of the Customs Register of Intellectual Property Right Objects that are protected under the Law.
Penalties for the violations prescribed by Articles 469, 470, 471, 472, 474, 475, 476, 477, 478, 479, 480, 481, 482, 483, 484 and 485 of the Customs Code of Ukraine.
Cоnfiscation of goods for the violations prescribed by Articles 471, 472, 473, 476, 482 and 483 of the Customs Code of Ukraine.
Conduction of in office audits and documentary inspections by the Customs after release of goods, with the follow-up additional charging of obligatory customs fees in case of incompliance with the legal regulatory acts.
Finding out an inconsistent information in a delivery control document or TIR, shipping and forwarding documents, regarding weight, title or cost of goods, a country of origin of goods.
Finding out corrections and erasures in a delivery control document or TIR, shipping and forwarding documents, which gave not been certified in accordance to the prescribed procedure.
Failoure to provide even one of the documents required for the customs clearance purposes.
Declaration in the customs declaration of the goods that belong to a «group of risks» or a group of «cover» (the list is specified by the SCSU).
Substential difference between a gross weight and net weight of goods that are forwarded in one vehicle, carrier or container.
Inconsistence of the data in an electronic notice from a Customs Authority, a postal item, a delivery control document or TIR, with the data declared in a Cargo Customs Declaration, if these inconsistent data will cause decreasing of customs fees and duties to be paid.
Nikolai Krasnov, 27 str., Kyiv, Ukraine 03115
044 220-45-67
About the Company
Useful Info
Services Packages
Foreign Trade Agent
Legal Support
FEA Consulting
Customs Brokerage
Non-tariff Regulation
Customs Value
Goods Classification
Door to door
Customs Warehouse
Placing Goods at TSW
and Maintenance of the Site