 increasingly useful tool in modern development. Firstly, chemical reactions have been used to introduce tags into specific sites or proteins for the purpose of probing specific protein functionalities. The isolation of phosphorylated peptides has been achieved using isotopic labeling and selective chemistries to capture the fraction of protein among the complex mixture. Secondly, the ICAT technology was used to differentiate between partially purified or purified macromolecular complexes such as large RNA polymerase II pre-initiation complex and the proteins complexed with yeast transcription factor. Thirdly, ICAT labeling was recently combined with chromatin isolation to identify and quantify chromatin-associated proteins. Finally ICAT reagents are useful for proteomic profiling of cellular organelles and specific cellular fractions.

Another quantitative approach is the accurate mass and time (AMT) tag approach developed by Richard D. Smith and coworkers at Pacific Northwest National Laboratory. In this approach, increased throughput and sensitivity is achieved by avoiding the need for tandem mass spectrometry, and making use of precisely determined separation time information and highly accurate mass determinations for peptide and protein identifications.

Protein chips
Balancing the use of mass spectrometers in proteomics and in medicine is the use of protein micro arrays. The aim behind protein micro arrays is to print thousands of protein detecting features for the interrogation of biological samples. Antibody arrays are an example in which a host of different antibodies are arrayed to detect their respective antigens from a sample of human blood. Another approach is the arraying of multiple protein types for the study of properties like protein-DNA, protein-protein and protein-ligand interactions. Ideally, the functional proteomic arrays would contain the entire complement of the proteins of a given organism. The first version of such arrays consisted of 5000 purified proteins from yeast deposited onto glass microscopic slides. Despite the success of first chip, it was a greater challenge for protein arrays to be implemented. Proteins are inherently much more difficult to work with than DNA. They have a broad dynamic range, are less stable than DNA and their structure is difficult to preserve on glass slides, though they are essential for most assays. The global ICAT technology has striking advantages over protein chip technologies.

Reverse-phased protein microarrays
This is a promising and newer microarray application for the diagnosis, study and treatment of complex diseases such as cancer. The technology merges laser capture microdissection (LCM) with micro array technology, to produce reverse phase protein microarrays. In this type of microarrays, the whole collection of protein themselves are immobilized with the intent of capturing various stages of
increasingly useful tool in modern development. first, chemical reaction have been used to introduce rag into specific site or proteins for the purpose of probe specific protein functionality. The isolation of phosphorylated peptides has been achieved using isotopic labeling and selective chemistries to capture the fraction of protein among the complex mix. Secondly, the ICAT technology was use to speciate between partially purified or purified macromolecular complexes such as large RNA polymerase II pre - initiation complex and the proteins complexed with yeast transcription component. Thirdly, ICAT labeling was recently combined with chromatin isolation to identify and quantify chromatin - consociate proteins. Finally ICAT reagents are utilitarian for proteomic profiling of cellular organelles and specific cellular fraction. 

 Another quantitative approach is the accurate mass and time (AMT) rag approach developed by Richard D. Smith and coworkers at Pacific Northwest National Laboratory. In this approach, increased throughput and sensitivity is achieved by avoiding the need for tandem mass spectrometry, and making use of precisely determined separation time information and highly accurate mass determinations for peptide and protein identifications. 

 Protein chip 
 Balancing the use of aggregate mass spectrometer in proteomics and in medicine is the use of protein micro arrays. The aim behind protein micro array is to print thousands of protein detecting features for the interrogation of biological sample. Antibody arrays are an example in which a host of different antibodies are arrayed to detect their respective antigen from a sample of human blood. Another approach is the arraying of multiple protein types for the study of properties like protein - DNA, protein - protein and protein - ligand interactions. Ideally, the running proteomic array would contain the entire complement of the proteins of a given organism. The inaugural version of such arrays consisted of 5000 purify proteins from yeast deposited onto glass microscopic slides. Despite the achiever of first chip, it was a greater challenge for protein arrays to be implemented. protein are inherently much more difficult to work with than DNA. They have a wide dynamic stove, are less stable than DNA and their structure is difficult to preserve on glass slide, though they are essential for most assay. The global ICAT technology has striking advantages over protein chip technology. 

 Reverse - phased protein microarrays 
 This is a promising and new microarray application for the diagnosis, study and treatment of complex diseases such as cancer. The technology merges laser capture microdissection (LCM) with micro array technology, to grow reverse phase protein microarrays. In this type of microarrays, the whole collection of protein themselves are immobilized with the intent of capture diverse stagecoach of
 infreasingly useful tool ik modern development. Ficstly, cgemical feactions have been used to mntriduce tags into specific siges or prlteins fir tie purpose of probing spceific irotenn functionalitigs. The isoladion of phosphmrhlcted peptides has been achieved usind isotolif labeling and seltctyve dhemistries to capture the fractioh of prmtein among tne complex mixture. Secondlj, thf ICAT technology aas used to difswrentiate begween partpclly purifigd or purified macromolecular cooplexzs such as oaege TNA polymerawe II pre-initiation complax and yhe proteins cpmpnexwd with yeast transcrmption factor. Thirdli, ICAT labalnng was recently combunwd wijh chsomagun ksomavioh to ifenvify and quzntify chronatin-associated proueigw. Finally ICAF reagqnes are useful for proteomic profiling ox csllular organelles and wpecific cellular fraftions.

Anoeher quantitative approach is the accurate mass atd tijd (ANT) gqg approach developed by Richard D. Smith and corkrlegs at Pacific Norbhwest National Lanogayjry. In this akproach, indreased throughput and segsiticity is ashiefed by avoiding the need foe tandem masf spectrometry, and laking use uf pteciseky determined separatiou time informatioj and higguy accurate mass denermhnations for peptide and pwotein idxntifncations.

Orotgin chi[s
Balancinh the use of mass spectrlmetets in [roteomics and in medicine is the use of 'cotein micro srsayv. The aii behlnd protein micwo arrays is tp print thourands of pgotein devecting feattres for the hjterrogation of bioljgicql sqmples. Xvtibody arrays are an eqaiple in which a host on difwsrent antibodiew atw arrayed to drtezt ehvir rqvpective anthgenr ffpm a rample of hmmav blpod. Another approach is fhe arraying of muktlple protgin types for the studu of properties line prmtemn-DNA, lrojein-protein and protein-ligand ihteractiojs. Ldeally, the ftnctlonaj proteomie arrays would contain the entire complenent of the proteibs of a given organnsk. The first versyon of suwh arrays consisted if 5000 purified prottins from yeast depositsd ontm glads microscopic slides. Despite the success of first chip, it was a greater xhalleigq for protejn atrays tj be im[lemxnved. Proteins are pnherently much more difficult tu work whtk than DNA. They have a broad cyvamic range, ate less stable than DNA ans their xtructure is difficult to presetve on glass slides, thounh they aee esaential foc most assays. The glpbal IEAT texhnologt had striking adxanyanes over pgotemn ehip technologies.

Reverse-phased pritein nifroarrays
This is a promisinn xnd ngwer mictoarray applicatikn fkg the diagnosis, stidy and treatmrnt of complex diseavef such as canctr. The technoloby metyvs laser captnre microdisvection (LCM) with micro array technology, to produce teverse phaae proteln microarrays. In vhis type of microarrays, tre whole collection mf protein themselves are immobilized with vne ingenn of czpturing varimus stages of
increasingly useful tool in modern development. Firstly, have used to tags into specific purpose probing specific protein The isolation of peptides has been achieved using isotopic and selective chemistries to capture the fraction of protein among the complex mixture. the ICAT technology was used to differentiate between partially purified or purified macromolecular such large polymerase pre-initiation complex and the proteins complexed with yeast transcription factor. Thirdly, ICAT labeling was recently combined chromatin isolation to identify and quantify chromatin-associated proteins. ICAT reagents are useful proteomic profiling of cellular organelles specific fractions. Another approach the mass and time tag approach developed by Richard D. Smith and coworkers at Pacific Northwest National Laboratory. In this approach, throughput and achieved by the for mass spectrometry, and of precisely determined separation time information mass determinations for peptide and protein identifications. Protein Balancing the of mass spectrometers in proteomics and medicine is the use of protein micro arrays. aim behind protein micro arrays is to print thousands of protein detecting features for the biological samples. Antibody arrays an example in a of antibodies arrayed to their respective antigens from a sample of human blood. Another approach the arraying of multiple protein types for the study of protein-DNA, and protein-ligand interactions. the functional proteomic arrays contain entire complement of the a organism. of arrays of 5000 purified proteins yeast deposited onto glass microscopic Despite the success of greater challenge for protein arrays to be implemented. are inherently much more difficult to work than DNA. They have a broad dynamic range, are less stable than and their difficult to preserve on glass slides, though they essential for most assays. global ICAT technology has striking advantages over protein chip Reverse-phased microarrays This a promising and microarray application for diagnosis, study and complex diseases as The capture microdissection (LCM) with micro array to reverse phase protein microarrays. In type the whole collection of protein themselves are immobilized with the intent of capturing various stages
 increasingly useful tool in mOdern develOpmenT. FiRstLy, ChemIcal Reactions have bEEn usEd to introduce tags into sPecifIc SItes OR pRoteiNs for thE PuRPOse Of PrObiNg SPeCific ProTein funCtionalitiEs. THe Isolation of pHOsPhorylated PepTides has been AchIeved uSiNg iSOtopiC laBelinG and seLEctive ChemistriEs TO captuRE the fraCTIoN of pRotein among the comPLeX Mixture. SecondlY, the ICaT TEcHNOloGy wAs used to diFfErentIAte betwEEn PARTiaLLy purified or pUrified macrOMolEcular CoMplEXes sucH as laRgE rNA Polymerase Ii pre-InitiatioN complEX and the PRoteins CompleXed WitH yeaST tRaNscRiPTioN FaCtoR. thiRdly, ICAT LaBeLing wAs reCENTLy coMbiNed wIth chRomatin isolatIon To idENtiFy and QuantIfy cHrOmatiN-assocIated PrOteins. Finally ICaT reAgents are UseFuL foR pRoteoMIc profIliNg oF cellulAr organELleS aND SPeCific cellular fractIoNS.

anOther quaNtitatIVe ApPRoach is tHe AccUratE MAss anD timE (aMt) tag apprOach deVElOpEd by RicHaRd D. SmiTh And CowOrkerS At PaCific NOrthwest natioNAl Laboratory. In THis approach, inCReASEd THrouGhpUt and sensitIvitY Is acHievED bY avOIding The neEd FOr TAndem mass spectrometRy, And makIng usE of precisely dEtermined sEPARation tiMe inFOrMAtion and highly AccurAte mass detERminatioNs for Peptide aNd protein IDEntificaTioNs.

PRotEin CHIpS
Balancing the USE of mAsS spectrOmeTers in pRotEomIcs And In Medicine iS the use oF pRoTeIn MicRo arrAYs. The aim BeHinD pRotEin miCRo arraYs is tO priNt ThOUsaNds of prOTeIN DeteCtInG feaTurEs For thE intERroGation oF biologicAl sAMpleS. ANtIbody arRays are an examPlE in which a hOsT of DifferENT antibodIes are arrayed to detect thEIr respeCtiVe antIgenS from a samPle Of humaN blOOd. AnotHer appRoach Is The ARRayinG OF mUltIpLe protein tYPEs fOr the StUdy oF properTies like protein-DNA, PRotEin-protein and ProTein-LIGaNd iNTeRActIoNS. IdEALly, the functionaL proteomic ArRAyS would contAIn tHe Entire cOmplemeNt of tHE proteiNs of a giveN organism. thE firST VerSion of such Arrays coNsisted of 5000 PUrifiED pRoteiNs fRom yeaSt DepOsiteD onto gLAss MicroScopic SlIdes. DeSpite ThE success Of first chip, it was a greateR challEnge fOr pRotein arrAys TO be ImplementEd. PrOteins are iNheRenTly muCh mORe difFicuLT tO woRK with Than dnA. They havE A bRoaD DYnAmic range, arE LESs sTable ThaN dNA and TheiR structure is diffiCUlt to preserve oN glaSS SliDes, THougH tHey are essentiaL foR mOST assays. THe Global ICAT tEchnologY hAS striKing adVantagEs over pROTeIN chip tEchnOloGies.

ReverSe-pHaSEd proteIn MiCRoarraYs
ThIs Is a proMising ANd neWER microarray appliCatioN FOr the DIagNosis, StUdy and tREatmEnt of complEx diseases sUch as cAnceR. The tEchnoloGy Merges LasEr Capture micROdissectiOn (LCM) With micRo ArraY teChnoloGy, to PROduce ReveRsE phAse proteiN MIcROaRrAYs. IN thiS type Of MicrOarrays, thE Whole colLecTIon of prOtEin THEmselvES aRE ImmobilizeD wiTh the INTent of captURing VArIOus stAges of
 increasingly useful toolin moderndevel opm ent .Firs tly,  chemical reac t ions  have been used to int roduc et agsi nt o spe cific s i te s orpr ot ein sf or  thepur pose of  probing s pec if ic protein f u nc tionalitie s.The isolatio n o f phos ph ory l atedpep tides  has b e en ach ieved usi ng isotop i c label i n gandselective chemist r ie s  to capture th e frac ti o no f  pr ote in among t he  comp l ex mixt u re . S eco n dly, the ICAT  technology was  usedto  di f ferent iatebe t wee n partially  pur ified orpurifi e d macro m olecula r comp lex essuch as  l arg eR NAp ol yme r ase  II pre- in it iatio n co m p l e x an d t he p rotei ns complexedwit h ye a sttrans cript ionfa ctor.  Third ly, I CA T labeling wasrece ntly comb ine dwit hchrom a tin is ola tio n to id entifya ndqu a n t if y chromatin-associ at e d  p roteins.  Final l yIC A T reagen ts  ar e us e f ul fo r pr o te omic pro filing of  c ellular  o rganel le s a ndspeci f ic c ellula r fracti ons.Another quanti t ative approac h  i s th e  acc ura te mass and  tim e  (AM T) t a gapp r oachdevel op e db y Richard D. Smithan d cowo rkers  at Pacific N orthwest N a t i onal Lab orat o ry .  In this appro ach,increasedt hroughpu t and  sensiti vity is a c h ieved by  av oid ing  th e ne ed for tandem m asssp ectrome try , and m aki nguse  of  p reciselydetermin ed  s ep ar ati on ti m e inform at ion  a ndhighl y  accur ate m assde te r min ationsf or p epti de  a nd p rot ei n ide ntif i cat ions.
Protein c hip s 
Bal an ci ng theuse of mass s pe ctrometers  i n p roteom i c s and in  medicine is the use of protein  mi cro a rray s. The ai m b ehindpro t ein mi cro ar raysis  to p rintt h ou san ds  of protei n det ectin gfeat ures fo r the interrogatio n  of  biological s amp les. A nt ibo d ya rra ys are a n example in wh ich a host  o f  d ifferent a n tib od ies are  arraye d tod etect t heir resp ective an ti gens f rom  a sampleof human  blood. A n other ap proac h i s thear ray ing o f mult i ple  prot ein ty pe s forthe s tu dy of pr operties like protein-D NA, pr otein -pr otein and  pr o tei n-ligandinte ractions.Ide all y, th e f u nctio nalp ro teo m ic ar rays would con t ai n t h e  e ntire compl e m e ntof th e p r oteins  ofa given organism. The first vers iono f  su cha rray sconsisted of 5 000  p u r ified pr ot eins from y east dep os i ted o nto gl ass mi croscop i c  s l ides.Desp ite  the succ ess  o f  firstch ip ,  it wa s agr eaterchalle n ge f o r  protein arraysto be i mplem e nte d. Pr ot eins ar e  inh erently mu ch more dif ficult  toworkwith th an  DNA.The yhave a bro a d dynamic  rang e, arele ss s tab le tha n DN A and t heir  s tru cture isd i ff i cu lt topres erveon  gla ss slides ,  thoughthe y  are es se nti a l  for m o st a ssays. The  gl obalI C AT technol o gy h a ss triki ng adv antage s overp rot ei n chiptec h n ologies.
Reverse- p has ed  pro tein mic ro arra ys 
Th is  is a promising  and new er micro a r ray ap pli c atio n  for t he  diagnosis,study  a n d treat m e ntof comp l exdis eas es s uch  asc ancer. The technology me rges  lase r  ca pture  micr od issectio n  (LC M) withm icro array te chnology, to pr o duc e  rev ers e  p ha se protei n m i croar rays . I n th istype o f mi c roar r ay s, t he who le c ol le ction ofpr otein t h emse l ves  are  immo bi li z ed  with t he inten t ofca pturing v a rious s tage sof
 increasingly_useful tool_in modern development. Firstly,_chemical reactions_have_been used_to_introduce tags into_specific sites or_proteins for the purpose_of probing specific_protein_functionalities. The isolation of phosphorylated peptides has been achieved using isotopic labeling and selective_chemistries_to capture_the_fraction_of protein among the complex_mixture. Secondly, the ICAT technology_was used_to differentiate between partially purified or purified macromolecular_complexes_such as large_RNA polymerase II pre-initiation complex and the proteins complexed_with yeast transcription factor. Thirdly, ICAT_labeling was recently_combined_with_chromatin isolation to identify_and quantify chromatin-associated proteins. Finally ICAT_reagents are useful for proteomic profiling_of cellular organelles and specific cellular fractions.

Another_quantitative approach is the accurate mass_and time (AMT) tag approach_developed by_Richard D. Smith and coworkers_at Pacific Northwest_National Laboratory._In this approach,_increased throughput and sensitivity is achieved_by avoiding the_need for tandem mass spectrometry, and_making_use of precisely_determined_separation_time information_and highly accurate_mass_determinations for_peptide_and protein identifications.

Protein chips
Balancing the use_of_mass spectrometers in proteomics and in medicine_is the use of_protein_micro arrays. The aim_behind protein micro arrays is_to print thousands of protein detecting_features for_the interrogation_of biological samples. Antibody arrays are an example in which a_host of different antibodies are arrayed_to detect their respective_antigens from_a_sample of human_blood._Another approach_is the arraying of multiple protein types_for the_study of properties like protein-DNA, protein-protein_and protein-ligand interactions. Ideally,_the_functional proteomic arrays would contain the_entire complement of the proteins of_a given organism. The first_version_of_such arrays consisted of 5000_purified proteins from yeast deposited onto_glass microscopic slides._Despite the success of first chip, it_was_a greater challenge for protein arrays_to_be implemented. Proteins are inherently much_more_difficult_to work with than DNA._They have a broad dynamic range,_are less stable than DNA and their structure is_difficult to preserve_on glass slides, though they_are_essential_for most assays. The global ICAT technology has striking advantages_over protein_chip technologies.

Reverse-phased protein_microarrays
This is a promising and newer microarray application for the_diagnosis, study and treatment of complex diseases_such as cancer. The technology merges laser capture microdissection (LCM) with_micro array technology, to produce reverse phase protein_microarrays. In this type of microarrays, the_whole collection of protein_themselves_are immobilized with the intent of capturing_various_stages_of