Title of Invention: Anti-TMEM106B antibodies and methods of use thereof Abstract: The present disclosure is generally directed to compositions that include antibodies, e.g., monoclonal antibodies, antibody fragments, etc., that specifically bind a TMEM106B polypeptide, e.g., a mammalian TMEM106B or human TMEM106B, and use of such compositions in preventing, reducing risk, or treating an individual in need thereof. Detailed Description: Part general_description_paragraphs: Part CROSS-REFERENCE TO RELATED APPLICATIONS: This application is a national phase entry of International Application No. PCT/US2018/067236, filed Dec. 21, 2018, which claims the benefit of U.S. Provisional Application No. 62/612,098, filed Dec. 29, 2017, which is hereby incorporated by reference in its entirety. Part SUBMISSION OF SEQUENCE LISTING ON ASCII TEXT FILE: The content of the following submission on ASCII text file is incorporated herein by reference in its entirety: a computer readable form (CRF) of the Sequence Listing (file name: 735022002040SEQLIST.TXT, date recorded: Dec. 19, 2018, size: 169 KB). Part FIELD OF THE PRESENT DISCLOSURE: The present disclosure relates to anti-TMEM106B antibodies and therapeutic uses of such antibodies. Part BACKGROUND OF THE PRESENT DISCLOSURE: Transmembrane protein 106B (TMEM106B) is a type 2 single pass transmembrane glycoprotein residing primarily within the membrane of late endosome and lysosomes. (See, e.g., Lang et al., 2012, J Biol Chem, 287:19355-19365; Chen-Plotkin et al., 2012, J Neurosci, 32:11213-11227; Brady et al., 2013, Human Molecular Genetics, 22:685-695.) TMEM106B is widely expressed in human tissue, and of particular interest expressed in neurons, glial cells, and endothelial and pen-vascular cells in the brain. TMEM106B is highly conserved in mammals, with the human protein sharing 99% sequence identity with the cynomolgus variant and 97% sequence identify with the murine ortholog. TMEM106B has a cytoplasmic domain predicted to range from amino acid residues 1-92 (of human TMEM106B; SEQ ID NO: 1), a transmembrane domain predicted to range from amino acid residues 96-117, and a lumenal domain predicted to range from amino acid residues 118-274. Five sequence motifs of post-translational N-glycosylation sites (N-X-T/S) span its lumenal domain. Simple glycans are added to three of the asparagine residues (N145, N151, and N164) and are not critical for TMEM106B localization. Complex glycans are added to the most C-terminal motifs at N183 and N256; loss of complex glycans on N183 impairs TMEM106B forward transport to endosomes/lysosomes and results in endoplasmic retention. Additionally, N256 complex glycosylation is necessary for proper TMEM106B sorting. (See, e.g., Nicholson and Rademakers, 2016, Acta Neuropathol, 132:639-651.) The function of TMEM106B has not been fully characterized. Recent reports have indicated a role of TMEM106B in dendrite branching, morphogenesis, and maintenance by inhibiting trafficking of lysosomes along dendrites. (See, e.g., Brady et al., 2013, Human Molecular Genetics, 126:696-698; Schwenk et al., 2014, EMBO J, 33:450-467; Clayton et al., 2018, Brain 141(12): 3428-3442.) TMEM106B has been shown to interact with various proteins, including without limitation progranulin protein (GRN), other TMEM106 protein family members, such as TMEM106A and TMEM106C, clathrin heavy chain (CLTC), the 1 subunit of adipocyte protein 2 (AP2M1), charged multi-vesicular body protein 2b (CHMP2B), microtubule-associated protein 6 (MAP6), lysosomal-associated membrane protein 1 (LAMP1), and vacuolar-ATPase subunit accessory protein 1 (v-ATPase Ap1). TMEM106B has been genetically linked to various disorders and diseases, in particular neurodegenerative disorders. Such disorders include, without limitation, conditions characterized by the presence of pathological TDP-43 inclusions (i.e., TDP-43 proteinopathies; transactive response DNA binding protein 43), Frontotemporal lobar degeneration (FTLD), FTLD with TDP-43 inclusions (FTLD-TDP), including FTLD-TDP caused by progranulin (GRN) or C90rf72 mutations, TDP-43 proteinopathies, Alzheimer's disease. Lewy body dementia (LBD), hippocampal sclerosis (HpScl), hippocampal sclerosis of aging (HS-Aging), hypomyelinating leukodystrophies, and cognitive impairment in various disorders, such as amyotrophic lateral sclerosis (ALS). TMEM106B has also been linked to metastasis in non-small cell lung cancer (Kundu et al., 2016; Nature Commun. 2018; 9: 2731, Cancer Research, Proceedings of the 107th Annual Meeting of the American Association for Cancer Research, abstract no. 688). TMEM106B has also been linked to chronic traumatic encephalopathy (CTE)-related neuropathology and dementia in CTE patients, including changes in AT8 tau deposition, CD68 cell density and PSD-95 concentration (Cherry et al., 2018, Acta Neuropathol Commun. 6:115). Accordingly, there is a need for therapies targeting TMEM106B, including therapeutic antibodies that specifically bind TMEM106B, and/or therapies that are capable of inhibiting the activity of TMEM106B, such as by reducing TMEM106B protein levels or function or by blocking or reducing the binding of TMEM106B to one or more of its ligands or binding partners, or otherwise modulate the effective concentration of one or more of its ligands or binding partners, in order to treat various diseases, disorders, and conditions associated with TMEM106B activity. All references cited herein, including patent applications and publications, are hereby incorporated by reference in their entirety. Part SUMMARY OF THE PRESENT DISCLOSURE: The present disclosure is generally directed to anti-TMEM106B antibodies and methods of using such antibodies. The methods provided herein find use in preventing, reducing risk, or treating an individual having a neurodegenerative disease, disorder, or condition. In some embodiments, the present invention provides a method for preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of a neurodegenerative disorder, a disorder characterized by the presence of TDP-43 inclusions, a TDP-43 proteinopathy, inflammatory cell debris or protein aggregates, abnormal circulating myeloid cells, unhealthy aging, frontotemporal lobar degeneration (FTLD), frontotemporal dementia (FTD), FTD with progranulin mutations, FTD with C90rf72 mutations, frontotemporal lobar degeneration with TDP-43 inclusions, hippocampal sclerosis (HpScl), hippocampal sclerosis of aging (HS-Aging), Alzheimer's disease, Lewy body dementia, cognitive impairment, age related cognitive impairment, age related brain atrophy, age-associated traits, including without limitations inflammation, neuronal loss, and cognitive deficits, such as cognitive defects in the absence of known brain disease, including cognitive deficits of the frontal cerebral cortex of older individuals, cognitive impairment in amyotrophic lateral sclerosis, cognitive impairment in chronic traumatic encephalopathy (CTE), diseases, disorders, and conditions associated with over expression or increased activity of TMEM106B, a hypomyelinating disorder, cancer, and metastasis the method comprising administering to an individual in need thereof a therapeutically effective amount of an anti-TMEM106B antibody. Accordingly, certain aspects of the present disclosure relate to an isolated (e.g., monoclonal) anti-TMEM106B antibody, wherein the anti-TMEM106B antibody has a property selected from the group consisting of: decreasing cellular levels of TMEM106B, decreasing intracellular levels of TMEM106B, inhibiting or reducing the interaction between TMEM106B and one or more of its ligand or binding proteins, and any combination thereof. In certain embodiments that may be combined with any of the preceding embodiments, the antibody decreases cell surface levels of TMEM106B, decreases intracellular levels of TMEM106B, decreases total levels of TMEM106B, decreases endosomal levels of TMEM106B, decreases lysosomal levels of TMEM106B, or any combination thereof. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody induces TMEM106B degradation, TMWM106B cleavage, TMEM106B internalization, TMEM106B down regulation, or any combination thereof. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in vivo. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in brain. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in one or more peripheral organs. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in brain, one or more peripheral organs, or any combination thereof. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in microglia. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody decreases cellular levels of TMEM106B in neurons. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody inhibits or reduces one or more interactions between TMEM106B and progranulin protein, other TMEM106 protein family members, such as TMEM106B and TMEM106C, clathrin heavy chain (CLTC), the 1 subunit of adipocyte protein 2 (AP2M1), CHMP2B, microtubule-associated protein 6 (MAP6), lysosomal-associated membrane protein 1 (LAMP1), vacuolar-ATPase subunit accessory protein 1, or any protein or polypeptide that modulates the function of TMEM106B. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure binds a discontinuous TMEM106B epitope. In certain embodiments that may be combined with any of the preceding embodiments, the discontinuous TMEM106B epitope comprises two or more peptides, three or more peptides, four or more peptides, five or more peptides, six or more peptides, seven or more peptides, eight or more peptides, nine or more peptides, or 10 or more peptides. In certain embodiments that may be combined with any of the preceding embodiments, each of the peptides comprise five or more, six or more, seven or more, eight or more, nine or more, 10 or more, 11 or more, 12 or more, 13 or more 14 or more, 15 or more, 16 or more, 17 or more, 18 or more, 19 or more, 20 or more, 21 or more, 22 or more, 23 or more, 24 or more, 25 or more, 26 or more, 27 or more, 28 or more, 29 or more, or 30 or more amino acid residues of the amino acid sequence of SEQ ID NO: 1, of the amino acid sequence of SEQ ID NO:2, or of the amino acid sequence of SEQ ID NO:315; or five or more, six or more, seven or more, eight or more, nine or more, 10 or more, 11 or more, 12 or more, 13 or more 14 or more, 15 or more, 16 or more, 17 or more, 18 or more, 19 or more, 20 or more, 21 or more, 22 or more, 23 or more, 24 or more, 25 or more, 26 or more, 27 or more, 28 or more, 29 or more, or 30 or more amino acid residues on a mammalian TMEM106B protein corresponding to the amino acid sequence of SEQ ID NO: 1, to the amino acid sequence of SEQ ID NO:2, or to the amino acid sequence of SEQ ID NO:315. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure binds to a conformational epitope of TMEM106B. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure competes with one or more reference anti-TMEM106B antibodies selected from the group consisting of TM-1, TM-17, TM-22, TM-23, TM-26, and TM-27, and any combination thereof for binding to TMEM106B. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure competes with one or more reference anti-TMEM106B antibodies selected from the group consisting of TM-2, TM-3, TM-5, TM-7, TM-9, TM-10, TM-11, TM-12, TM-13, TM-18, TM-19, TM-21, TM-25, TM-28, TM-29, TM-32, TM-35, TM-37, TM-39, TM-42, TM-45, TM-48, and TM-53, and any combination thereof for binding to TMEM106B. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure competes with one or more reference anti-TMEM106B antibodies selected from the group consisting of TM-4, TM-6, TM-8, TM-14, TM-15, TM-16, TM-20, TM-31, TM-33, TM-34, TM-36, TM-41, TM-44, TM-46, TM-47, TM-49, TM-50, TM-51, TM-52, and any combination thereof for binding to TMEM106B. In some embodiments, the reference anti-TMEM106B antibody comprises the VH and VL of the antibody selected from the group consisting of TM-4, TM-6, TM-8, TM-14, TM-15, TM-16, TM-20, TM-31, TM-33, TM-34, TM-36, TM-41, TM-44, TM-46, TM-47, TM-49, TM-50, TM-51, TM-52, and any combination thereof. Other aspects of the present disclosure relate to an isolated (e.g., monoclonal) anti-TMEM106B antibody, wherein the anti-TMEM106B antibody comprises at least one, two, three, four, five, or six HVRs of an antibody selected from the group consisting of: TM-1, TM-2, TM-3, TM-4, TM-5, TM-6, TM-7, TM-8, TM-9, TM-10, TM-11, TM-12, TM-13, TM-14, TM-15, TM-16, TM-17, TM-18, TM-19, TM-20, TM-21, TM-22, TM-23, TM-24, TM-25, TM-26, TM-27, TM-28, TM-29, TM-30, TM-31, TM-32, TM-33, TM-34, TM-35, TM-36, TM-37, TM-38, TM-39, TM-40, TM-41, TM-42, TM-43, TM-44, TM-45, TM-46, TM-47, TM-48, TM-49, TM-50, TM-51, TM-52, and TM-53. In some embodiments, the anti-TMEM106B antibody comprises the six HVR (e.g., as shown in Table 4A below) of the antibody selected from the group consisting of TM-1, TM-2, TM-3, TM-4, TM-5, TM-6, TM-7, TM-8, TM-9, TM-10, TM-11, TM-12, TM-13, TM-14, TM-15, TM-16, TM-17, TM-18, TM-19, TM-20, TM-21, TM-22, TM-23, TM-24, TM-25, TM-26, TM-27, TM-28, TM-29, TM-30, TM-31, TM-32, TM-33, TM-34, TM-35, TM-36, TM-37, TM-38, TM-39, TM-40, TM-41, TM-42, TM-43, TM-44, TM-45, TM-46, TM-47, TM-48, TM-49, TM-50, TM-51, TM-52, and TM-53. Other aspects of the present disclosure relate to an isolated (e.g., monoclonal) anti-TMEM106B antibody which binds essentially the same TMEM106B epitope as a reference anti-TMEM106B antibody comprising the six HVRs of an antibody selected from the group consisting of: TM-1, TM-2, TM-3, TM-4, TM-5, TM-6, TM-7, TM-8, TM-9, TM-10, TM-11, TM-12, TM-13, TM-14, TM-15, TM-16, TM-17, TM-18, TM-19, TM-20, TM-21, TM-22, TM-23, TM-24, TM-25, TM-26, TM-27, TM-28, TM-29, TM-30, TM-31, TM-32, TM-33, TM-34, TM-35, TM-36, TM-37, TM-38, TM-39, TM-40, TM-41, TM-42, TM-43, TM-44, TM-45, TM-46, TM-47, TM-48, TM-49, TM-50, TM-51, TM-52, and TM-53. In some embodiments, the reference anti-TMEM106B antibody comprises the VH and VL(e.g., as shown in Table 4B below) of the antibody selected from the group consisting of: TM-1, TM-2, TM-3, TM-4, TM-5, TM-6, TM-7, TM-8, TM-9, TM-10, TM-11, TM-12, TM-13, TM-14, TM-15, TM-16, TM-17, TM-18, TM-19, TM-20, TM-21, TM-22, TM-23, TM-24, TM-25, TM-26, TM-27, TM-28, TM-29, TM-30, TM-31, TM-32, TM-33, TM-34, TM-35, TM-36, TM-37, TM-38, TM-39, TM-40, TM-41, TM-42, TM-43, TM-44, TM-45, TM-46, TM-47, TM-48, TM-49, TM-50, TM-51, TM-52, and TM-53. Other aspects of the present disclosure relate to an isolated (e.g., monoclonal) anti-TMEM106B antibody which binds to one or more amino acids within amino acid residues 59-73, 80-90, 5-19, 59-69, 52-62, 64-74, 151-165, 185-195, 139-149, 248-258, 156-161, 202-207, 219-233, 126-140, 185-195, 260-274, 202-212, 151-161, 223-233, 143-153, 223-228, 133-145, and/or 198-212 of human TMEM106B (SEQ ID NO: 1). In some embodiments of the present disclosure, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 151-165 and/or 185-195. In some embodiments of the present disclosure, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 59-73, 80-90, 139-149, and/or 248-258 of human TMEM106B (SEQ ID NO: 1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 5-19, 156-161, 202-207, and/or 219-233 of human TMEM106B (SEQ ID NO: 1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 126-140, 185-195, and/or 260-274 of human TMEM106B (SEQ ID NO:1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 202-212 of human TMEM106B (SEQ ID NO:1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 151-161 and/or 223-233 of human TMEM106B (SEQ ID NO: 1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 59-69, 143-153, and/or 223-228 of human TMEM106B (SEQ ID NO: 1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 133-145 and/or 198-212 of human TMEM106B (SEQ ID NO: 1). In some embodiments, an anti-TMEM106B antibody binds to one or more amino acids within amino acid residues 52-62, 64-75, and/or 223-228 of human TMEM106B (SEQ ID NO: 1). Other aspects of the present disclosure relate to an isolated anti-TMEM106B antibody which binds to one or more amino acids within the amino acid sequence NITNNNYYSVEVENI (SEQ ID NO:324), TIIGPLDMKQI (SEQ ID NO:325), VTCPTCQGTGRIPRG (SEQ ID NO:326), (ALIPYSDQRLR (SEQ ID NO:327), (KRTIYLNITNT (SEQ ID NO:328), YQYVDCGRNTT (SEQ ID NO:329), (LSHLPLHSSKEDAYD (SEQ ID NO:332), (NYYSVE (SEQ ID NO:334), (VIAEEM (SEQ ID NO:335), (IKVHNIVLMMQVTVT; SEQ ID NO:336), (IGVKSAYVSYDVQKR; SEQ ID NO:337), (QLGQSEYLNVLQPQQ (SEQ ID NO:338), (VIAEEMSYMYD (SEQ ID NO:340), (NITNNNYYSVE (SEQ ID NO:341), (NIVLMMQVTV (SEQ ID NO:342), (VTCPTCQGTGR (SEQ ID NO:343), (YLNITNTLNIT (SEQ ID NO:344), (NIVLMM (SEQ ID NO:345), (VSYDVQKRTIYLN (SEQ ID NO:346), (TVPTVIAEEMSYMYD (SEQ ID NO:347), (EFTGRDSVTCP (SEQ ID NO:348), and/or (CQGTGRIPRGQE (SEQ ID NO:349). In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody further inhibits interaction between TMEM106B and one or more of its ligands, signaling proteins or binding proteins by: a) reducing the effective levels of TMEM106B available for interacting with the one or more ligands or binding proteins; b); blocking one or more of the sites on TMEM106B required for interaction with the one or more ligands or binding proteins; c) preventing one or more posttranslational events on TMEM106B that are required for interaction with the one or more ligands or binding proteins and/or for correct processing and/or subcellular localization of TMEM106B; d) inducing degradation of TMEM106B; e) changing the conformation of TMEM106B, or both. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody binds specifically to human TMEM106B, mouse TMEM106B, cyno TMEM106B, or a combination thereof. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody is a human antibody, a humanized antibody, a bispecific antibody, a monoclonal antibody, a multivalent antibody, a conjugated antibody, or a chimeric antibody. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody is a bispecific antibody recognizing a first antigen and a second antigen. In certain embodiments that may be combined with any of the preceding embodiments, the first antigen is TMEM106B and the second antigen is an antigen facilitating transport across the blood-brain-barrier. In certain embodiments that may be combined with any of the preceding embodiments, the second antigen is selected from the group consisting of TMEM106B, transferrin receptor (TR), insulin receptor (HIR), insulin-like growth factor receptor (IGFR), low-density lipoprotein receptor related proteins 1 and 2 (LPR-1 and 2), diphtheria toxin receptor, CRM197, a llama single domain antibody, TMEM 30(A), a protein transduction domain, TAT, Syn-B, penetratin, a poly-arginine peptide, an angiopep peptide, basigin, Glut1, and CD98hc, and ANG1005. In certain embodiments that may be combined with any of the preceding embodiments, an anti-TMEM106B antibody of the present disclosure increases the expression of TGFbeta. In some embodiments that may be combined with any of the preceding embodiments, the antibody is a monoclonal antibody. In some embodiments that may be combined with any of the preceding embodiments, the antibody is of the IgG class, the IgM class, or the IgA class. In some embodiments, the antibody is of the IgG class and has an IgG1, IgG2, or IgG4 isotype. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody is an antibody fragment that binds to an epitope comprising amino acid residues on human TMEM106B or a mammalian TMEM106B protein. In certain embodiments that may be combined with any of the preceding embodiments, the fragment is a Fab, Fab′, Fab′-SH, F(ab′)2, Fv, or scFv fragment. In some embodiments that may be combined with any of the preceding embodiments, the antibody is a humanized antibody or a chimeric antibody. Other aspects of the present disclosure relate to an isolated nucleic acid comprising a nucleic acid sequence encoding the anti-TMEM106B antibody of any of the preceding embodiments. Other aspects of the present disclosure relate to a vector comprising the nucleic acid of any of the preceding embodiments. Other aspects of the present disclosure relate to an isolated host cell comprising the vector of any of the preceding embodiments. Other aspects of the present disclosure relate to a method of producing an anti-TMEM106B antibody, comprising culturing the host cell of any of the preceding embodiments so that the anti-TMEM106B antibody is produced. In certain embodiments, the method further comprises recovering the anti-TMEM106B antibody produced by the host cell. Other aspects of the present disclosure relate to an isolated anti-TMEM106B antibody produced by the method of any of the preceding embodiments. Other aspects of the present disclosure relate to a pharmaceutical composition comprising the anti-TMEM106B antibody of any of the preceding embodiments, and a pharmaceutically acceptable carrier. Other aspects of the present disclosure relate to a method of preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, a traumatic brain injury, a spinal cord injury, long-term depression, atherosclerotic vascular diseases, undesirable symptoms of normal aging, dementia, mixed dementia, Creutzfeldt-Jakob disease, normal pressure hydrocephalus, amyotrophic lateral sclerosis, Huntington's disease, taupathy disease, stroke, acute trauma, chronic trauma, lupus, acute and chronic colitis, Crohn's disease, inflammatory bowel disease, ulcerative colitis, malaria, essential tremor, central nervous system lupus, Behcet's disease, Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, degenerative disc disease, Shy-Drager syndrome, progressive supranuclear palsy, cortical basal ganglionic degeneration, acute disseminated encephalomyelitis, granulomartous disorders, Sarcoidosis, diseases of aging, age related macular degeneration, glaucoma, retinitis pigmentosa, retinal degeneration, respiratory tract infection, sepsis, eye infection, systemic infection, inflammatory disorders, arthritis, multiple sclerosis, metabolic disorder, obesity, insulin resistance, type 2 diabetes, tissue or vascular damage, an injury, inflammatory cell debris or protein aggregates, abnormal circulating myeloid cells, unhealthy aging, age-related cognitive impairment, age-related brain atrophy, age-associated traits, including without limitation inflammation, neuronal loss, and cognitive deficits, such as cognitive deficits in the absence of known brain disease, including cognitive deficits of the frontal cerebral cortex of an older individual and, one or more undesirable symptoms of normal aging, comprising administering to the individual a therapeutically effective amount of the anti-TMEM106B antibody of any of the preceding embodiments. Other aspects of the present disclosure relate to an anti-TMEM106B antibody of any of the preceding embodiments for use in preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, a traumatic brain injury, a spinal cord injury, long-term depression, atherosclerotic vascular diseases, undesirable symptoms of normal aging, dementia, mixed dementia, Creutzfeldt-Jakob disease, normal pressure hydrocephalus, amyotrophic lateral sclerosis, Huntington's disease, taupathy disease, stroke, acute trauma, chronic trauma, lupus, acute and chronic colitis, Crohn's disease, inflammatory bowel disease, ulcerative colitis, malaria, essential tremor, central nervous system lupus, Behcet's disease, Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, degenerative disc disease, Shy-Drager syndrome, progressive supranuclear palsy, cortical basal ganglionic degeneration, acute disseminated encephalomyelitis, granulomartous disorders, Sarcoidosis, diseases of aging, age related macular degeneration, glaucoma, retinitis pigmentosa, retinal degeneration, respiratory tract infection, sepsis, eye infection, systemic infection, inflammatory disorders, arthritis, multiple sclerosis, metabolic disorder, obesity, insulin resistance, type 2 diabetes, tissue or vascular damage, an injury, inflammatory cell debris or protein aggregates, abnormal circulating myeloid cells, unhealthy aging, age-related cognitive impairment, age-related brain atrophy, age-associated traits, including without limitation inflammation, neuronal loss, and cognitive deficits, such as cognitive deficits in the absence of known brain disease, including cognitive deficits of the frontal cerebral cortex of older individual, and one or more undesirable symptoms of normal aging. Other aspects of the present disclosure relate to an anti-TMEM106B antibody of any of the preceding embodiments for use in preventing or reducing metastasis. Other aspects of the present disclosure relate to an anti-TMEM106B antibody of any of the preceding embodiments for use in preventing, reducing risk, or treating an individual having cancer. Other aspects of the present disclosure relate to use of an anti-TMEM106B antibody of any of the preceding embodiments in the manufacture of a medicament for preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, a traumatic brain injury, a spinal cord injury, long-term depression, atherosclerotic vascular diseases, undesirable symptoms of normal aging, dementia, mixed dementia, Creutzfeldt-Jakob disease, normal pressure hydrocephalus, amyotrophic lateral sclerosis, Huntington's disease, taupathy disease, stroke, acute trauma, chronic trauma, lupus, acute and chronic colitis, Crohn's disease, inflammatory bowel disease, ulcerative colitis, malaria, essential tremor, central nervous system lupus, Behcet's disease, Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, degenerative disc disease, Shy-Drager syndrome, progressive supranuclear palsy, cortical basal ganglionic degeneration, acute disseminated encephalomyelitis, granulomartous disorders, Sarcoidosis, diseases of aging, age related macular degeneration, glaucoma, retinitis pigmentosa, retinal degeneration, respiratory tract infection, sepsis, eye infection, systemic infection, inflammatory disorders, arthritis, multiple sclerosis, metabolic disorder, obesity, insulin resistance, type 2 diabetes, tissue or vascular damage, an injury, inflammatory cell debris or protein aggregates, abnormal circulating myeloid cells, unhealthy aging, age-related cognitive impairment, age-related brain atrophy, age-associated traits, including without limitations inflammation, neuronal loss, and cognitive deficits, such as cognitive deficits in the absence of known brain disease, including cognitive deficits of the frontal cerebral cortex of older individual and one or more undesirable symptoms of normal aging. Other aspects of the present disclosure relate to a method of preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, progressive supranuclear palsy, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, amyotrophic lateral sclerosis, traumatic brain injury, a spinal cord injury, dementia, stroke, Parkinson's disease, acute disseminated encephalomyelitis, retinal degeneration, age related macular degeneration, glaucoma, multiple sclerosis, septic shock, bacterial infection, arthritis, and osteoarthritis, comprising administering to the individual a therapeutically effective amount of the anti-TMEM106B antibody of any of the preceding embodiments. Other aspects of the present disclosure relate to an anti-TMEM106B antibody of any of the preceding embodiments for use in preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, progressive supranuclear palsy, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, amyotrophic lateral sclerosis, traumatic brain injury, a spinal cord injury, dementia, stroke, Parkinson's disease, acute disseminated encephalomyelitis, retinal degeneration, age related macular degeneration, glaucoma, multiple sclerosis, septic shock, bacterial infection, arthritis, and osteoarthritis. Other aspects of the present disclosure relate to use of an anti-TMEM106B antibody of any of the preceding embodiments in the manufacture of a medicament for preventing, reducing risk, or treating an individual having a disease, disorder, or injury selected from the group consisting of frontotemporal dementia, progressive supranuclear palsy, Alzheimer's disease, vascular dementia, seizures, retinal dystrophy, amyotrophic lateral sclerosis, traumatic brain injury, a spinal cord injury, dementia, stroke, Parkinson's disease, acute disseminated encephalomyelitis, retinal degeneration, age related macular degeneration, glaucoma, multiple sclerosis, septic shock, bacterial infection, arthritis, and osteoarthritis. In certain embodiments that may be combined with any of the preceding embodiments, the anti-TMEM106B antibody comprises two or more anti-TMEM106B antibodies. It is to be understood that one, some, or all of the properties of the various embodiments described herein may be combined to form other embodiments of the present invention. These and other aspects of the invention will become apparent to one of skill in the art. These and other embodiments of the invention are further described by the detailed description that follows. Part DETAILED DESCRIPTION OF THE PRESENT DISCLOSURE: The present disclosure relates to anti-TMEM106B antibodies (e.g., monoclonal antibodies); methods of making and using such antibodies; pharmaceutical compositions comprising such antibodies; nucleic acids encoding such antibodies; and host cells comprising nucleic acids encoding such antibodies. The techniques and procedures described or referenced herein are generally well understood and commonly employed using conventional methodology by those skilled in the art, such as, for example, the widely utilized methodologies such as those described in Sambrook et al. Molecular Cloning: A Laboratory Manual 3d edition (2001) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Current Protocols in Molecular Biology (F. M. Ausubel, et al. eds., (2003); Monoclonal Antibodies: A Practical Approach (P. Shepherd and C. Dean, eds., Oxford University Press, 2000). Part I. Definitions: The terms “TMEM106B” or “TMEM106B polypeptide” are used interchangeably herein refer herein to any native TMEM106B from any vertebrate source, including mammals such as primates (e.g., humans and cynos) and rodents (e.g., mice and rats), unless otherwise indicated. In some embodiments, the term encompasses both wild-type sequences and naturally occurring variant sequences, e.g., splice variants or allelic variants. In some embodiments, the term encompasses “full-length,” unprocessed TMEM106B as well as any form of TMEM106B that results from processing in the cell. In some embodiments, the TMEM106B is human TMEM106B. In some embodiments, the amino acid sequence of an exemplary TMEM106B is Uniprot Accession No: Q9NUM4 as of Jun. 27, 2006. In some embodiments, the amino acid sequence of an exemplary human TMEM106B is SEQ ID NO: 1. The terms “anti-TMEM106B antibody,” an “antibody that binds to TMEM106B,” and “antibody that specifically binds TMEM106B” refer to an antibody that is capable of binding TMEM106B with sufficient affinity such that the antibody is useful as a diagnostic and/or therapeutic agent in targeting TMEM106B. In one embodiment, the extent of binding of an anti-TMEM106B antibody to an unrelated, non-TMEM106B polypeptide is less than about 10% of the binding of the antibody to TMEM106B as measured, e.g., by a radioimmunoassay (RIA). In certain embodiments, an antibody that binds to TMEM106B has a dissociation constant (KD) of <1 μM, <100 nM, <10 nM, <1 nM, <0.1 nM, <0.01 nM, or <0.001 nM (e.g., 10−8 M or less, e.g. from 10−8 M to 10−13 M, e.g., from 10−9 M to 10−13 M). In certain embodiments, an anti-TMEM106B antibody binds to an epitope of TMEM106B that is conserved among TMEM106B from different species. With regard to the binding of an antibody to a target molecule, the term “specific binding” or “specifically binds” or is “specific for” a particular polypeptide or an epitope on a particular polypeptide target means binding that is measurably different from a non-specific interaction. Specific binding can be measured, for example, by determining binding of a molecule compared to binding of a control molecule. For example, specific binding can be determined by competition with a control molecule that is similar to the target, for example, an excess of non-labeled target. In this case, specific binding is indicated if the binding of the labeled target to a probe is competitively inhibited by excess unlabeled target. The term “specific binding” or “specifically binds to” or is “specific for” a particular polypeptide or an epitope on a particular polypeptide target as used herein can be exhibited, for example, by a molecule having a KD for the target of about any of 10−4 M or lower, 10−5 M or lower, 10−6 M or lower, 10−7 M or lower, 10−8 M or lower, 10−9 M or lower, 10−10 M or lower, 10−11 M or lower, 10−12 M or lower or a KD in the range of 10−4 M to 10−6 M or 10−6 M to 10−10 M or 10−7 M to 10−9 M. As will be appreciated by the skilled artisan, affinity and KD values are inversely related. A high affinity for an antigen is measured by a low KD value. In one embodiment, the term “specific binding” refers to binding where a molecule binds to a particular polypeptide or epitope on a particular polypeptide without substantially binding to any other polypeptide or polypeptide epitope. The term “immunoglobulin” (Ig) is used interchangeably with “antibody” herein. The term “antibody” herein is used in the broadest sense and specially covers monoclonal antibodies, polyclonal antibodies, multispecific antibodies (e.g., bispecific antibodies) including those formed from at least two intact antibodies, and antibody fragments so long as they exhibit the desired biological activity. “Native antibodies” are usually heterotetrameric glycoproteins of about 150,000 Daltons, composed of two identical Light (“L”) chains and two identical heavy (“H”) chains. Each light chain is linked to a heavy chain by one covalent disulfide bond, while the number of disulfide linkages varies among the heavy chains of different immunoglobulin isotypes. Each heavy and light chain also has regularly spaced intra-chain disulfide bridges. Each heavy chain has at one end a variable domain (VH) followed by a number of constant domains. Each light chain has a variable domain at one end (VL) and a constant domain at its other end; the constant domain of the light chain is aligned with the first constant domain of the heavy chain, and the light chain variable domain is aligned with the variable domain of the heavy chain. Particular amino acid residues are believed to form an interface between the light chain and heavy chain variable domains. For the structure and properties of the different classes of antibodies, see, e.g., Basic and Clinical Immunology, 8th Ed., Daniel P. Stites, Abba I. Terr and Tristram G. Parslow (eds.), Appleton & Lange, Norwalk, Conn., 1994, page 71 and Chapter 6. The light chain from any vertebrate species can be assigned to one of two clearly distinct types, called kappa (“κ”) and lambda (“λ”), based on the amino acid sequences of their constant domains. Depending on the amino acid sequence of the constant domain of their heavy chains (CH), immunoglobulins can be assigned to different classes or isotypes. There are five classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, having heavy chains designated alpha (“α”), delta (“δ”), epsilon (“ε”), gamma (“γ”), and mu (“μ”), respectively. The γ and α classes are further divided into subclasses (isotypes) on the basis of relatively minor differences in the CH sequence and function, e.g., humans express the following subclasses: IgG1, IgG2, IgG3, IgG4, IgA1, and IgA2. The subunit structures and three-dimensional configurations of different classes of immunoglobulins are well known and described generally in, for example, Abbas et al., Cellular and Molecular Immunology, 4th ed. (W.B. Saunders Co., 2000). The “variable region” or “variable domain” of an antibody, such as an anti-TMEM106B antibody of the present disclosure, refers to the amino-terminal domains of the heavy or light chain of the antibody. The variable domains of the heavy chain and light chain may be referred to as “VH” and “VL”, respectively. These domains are generally the most variable parts of the antibody (relative to other antibodies of the same class) and contain the antigen binding sites. The term “variable” refers to the fact that certain segments of the variable domains differ extensively in sequence among antibodies, such as anti-TMEM106B antibodies of the present disclosure. The variable domain mediates antigen binding and defines the specificity of a particular antibody for its particular antigen. However, the variability is not evenly distributed across the entire span of the variable domains. Instead, it is concentrated in three segments called hypervariable regions (HVRs) both in the light-chain and the heavy chain variable domains. The more highly conserved portions of variable domains are called the framework regions (FR). The variable domains of native heavy and light chains each comprise four FR regions, largely adopting a beta-sheet configuration, connected by three HVRs, which form loops connecting, and in some cases forming part of, the beta-sheet structure. The HVRs in each chain are held together in close proximity by the FR regions and, with the HVRs from the other chain, contribute to the formation of the antigen-binding site of antibodies (see Kabat et al., Sequences of Immunological Interest, Fifth Edition, National Institute of Health, Bethesda, Md. (1991)). The constant domains are not involved directly in the binding of antibody to an antigen, but exhibit various effector functions, such as participation of the antibody in antibody-dependent-cellular toxicity. The term “monoclonal antibody” as used herein refers to an antibody, such as a monoclonal anti-TMEM106B antibody of the present disclosure, obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical except for possible naturally occurring mutations and/or post-translation modifications (e.g., isomerizations, amidations, etc.) that may be present in minor amounts. Monoclonal antibodies are highly specific, being directed against a single antigenic site. In contrast to polyclonal antibody preparations which typically include different antibodies directed against different determinants (epitopes), each monoclonal antibody is directed against a single determinant on the antigen. In addition to their specificity, the monoclonal antibodies are advantageous in that they are synthesized by the hybridoma culture, uncontaminated by other immunoglobulins. The modifier “monoclonal” indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies to be used in accordance with the present invention may be made by a variety of techniques, including, for example, the hybridoma method, recombinant DNA methods, and technologies for producing human or human-like antibodies in animals that have parts or all of the human immunoglobulin loci or genes encoding human immunoglobulin sequences. The terms “full-length antibody,” “intact antibody” or “whole antibody” are used interchangeably to refer to an antibody, such as an anti-TMEM106B antibody of the present disclosure, in its substantially intact form, as opposed to an antibody fragment. Specifically, whole antibodies include those with heavy and light chains including an Fc region. The constant domains may be native sequence constant domains (e.g., human native sequence constant domains) or amino acid sequence variants thereof. In some cases, the intact antibody may have one or more effector functions. An “antibody fragment” refers to a molecule other than an intact antibody that comprises a portion of an intact antibody that binds the antigen to which the intact antibody binds. Examples of antibody fragments include Fab, Fab′, F(ab′)2 and Fv fragments; diabodies; linear antibodies (see U.S. Pat. No. 5,641,870, Example 2; Zapata et al., Protein Eng. 8(10):1057-1062 (1995)); single-chain antibody molecules and multispecific antibodies formed from antibody fragments. Papain digestion of antibodies, such as anti-TMEM106B antibodies of the present disclosure, produces two identical antigen-binding fragments, called “Fab” fragments, and a residual “Fc” fragment, a designation reflecting the ability to crystallize readily. The Fab fragment consists of an entire light chain along with the variable region domain of the heavy chain (VH), and the first constant domain of one heavy chain (CH1). Each Fab fragment is monovalent with respect to antigen binding, i.e., it has a single antigen-binding site. Pepsin treatment of an antibody yields a single large F(ab′)2 fragment which roughly corresponds to two disulfide linked Fab fragments having different antigen-binding activity and is still capable of cross-linking antigen. Fab′ fragments differ from Fab fragments by having a few additional residues at the carboxy terminus of the CH1 domain including one or more cysteines from the antibody hinge region. Fab′-SH is the designation herein for Fab′ in which the cysteine residue(s) of the constant domains bear a free thiol group. F(ab′)2 antibody fragments originally were produced as pairs of Fab′ fragments which have hinge cysteines between them. Other chemical couplings of antibody fragments are also known. The Fc fragment comprises the carboxy-terminal portions of both heavy chains held together by disulfides. The effector functions of antibodies are determined by sequences in the Fc region, the region which is also recognized by Fc receptors (FcR) found on certain types of cells. “Functional fragments” of antibodies, such as anti-TMEM106B antibodies of the present disclosure, comprise a portion of an intact antibody, generally including the antigen binding or variable region of the intact antibody or the Fc region of an antibody which retains or has modified FcR binding capability. Examples of antibody fragments include linear antibody, single-chain antibody molecules and multispecific antibodies formed from antibody fragments. The term “diabodies” refers to small antibody fragments prepared by constructing sFv fragments (see preceding paragraph) with short linkers (about 5-10) residues) between the VH and VL domains such that inter-chain but not intra-chain pairing of the variable domains is achieved, thereby resulting in a bivalent fragment, i.e., a fragment having two antigen-binding sites. Bispecific diabodies are heterodimers of two “crossover” sFv fragments in which the VH and VL domains of the two antibodies are present on different polypeptide chains. As used herein, a “chimeric antibody” refers to an antibody (immunoglobulin), such as a chimeric anti-TMEM106B antibody of the present disclosure, in which a portion of the heavy and/or light chain is identical with or homologous to corresponding sequences in antibodies derived from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chain(s) is(are) identical with or homologous to corresponding sequences in antibodies derived from another species or belonging to another antibody class or subclass, as well as fragments of such antibodies, so long as they exhibit the desired biological activity. Chimeric antibodies of interest herein include PRIMATIZED® antibodies wherein the antigen-binding region of the antibody is derived from an antibody produced by, e.g., immunizing macaque monkeys with an antigen of interest. As used herein, “humanized antibody” is used a subset of “chimeric antibodies.” “Humanized” forms of non-human (e.g., murine) antibodies, such as humanized forms of anti-TMEM106B antibodies of the present disclosure, are chimeric antibodies comprising amino acid residues from non-human HVRs and amino acid residues from human FRs. In certain embodiments, a humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the HVRs (e.g., CDRs) correspond to those of a non-human antibody, and all or substantially all of the FRs correspond to those of a human antibody. A humanized antibody optionally may comprise at least a portion of an antibody constant region derived from a human antibody. A “humanized form” of an antibody, e.g., a non-human antibody, refers to an antibody that has undergone humanization. A “human antibody” is one that possesses an amino-acid sequence corresponding to that of an antibody, such as an anti-TMEM106B antibody of the present disclosure, produced by a human and/or has been made using any of the techniques for making human antibodies as disclosed herein. This definition of a human antibody specifically excludes a humanized antibody comprising non-human antigen-binding residues. Human antibodies can be produced using various techniques known in the art, including phage-display libraries and yeast-display libraries. Human antibodies can be prepared by administering the antigen to a transgenic animal that has been modified to produce such antibodies in response to antigenic challenge, but whose endogenous loci have been disabled, e.g., immunized xenomice as well as generated via a human B-cell hybridoma technology. The term “hypervariable region,” “HVR,” or “HV,” when used herein refers to the regions of an antibody-variable domain, such as that of an anti-TMEM106B antibody of the present disclosure, that are hypervariable in sequence and/or form structurally defined loops. Generally, antibodies comprise six HVRs; three in the VH (H1, H2, H3), and three in the VL (L1, L2, L3). In native antibodies, H3 and L3 display the most diversity of the six HVRs, and H3 in particular is believed to play a unique role in conferring fine specificity to antibodies. Naturally occurring camelid antibodies consisting of a heavy chain only are functional and stable in the absence of light chain. A number of HVR delineations are in use and are encompassed herein. In some embodiments, the HVRs may be Kabat complementarity-determining regions (CDRs) based on sequence variability and are the most commonly used (Kabat et al., supra). In some embodiments, the HVRs may be Chothia CDRs. Chothia refers instead to the location of the structural loops (Chothia and Lesk J. Mol. Biol. 196:901-917 (1987)). In some embodiments, the HVRs may be AbM HVRs. The AbM HVRs represent a compromise between the Kabat CDRs and Chothia structural loops, and are used by Oxford Molecular's AbM antibody-modeling software. In some embodiments, the HVRs may be “contact” HVRs. The “contact” HVRs are based on an analysis of the available complex crystal structures. The residues from each of these HVRs are noted below. Loop Kabat AbM Chothia Contact Ll L24-L34 L24-L34 L26-L32 L30-L36 L2 L50-L56 L50-L56 L50-L52 L46-L55 L3 L89-L97 L89-L97 L91-L96 L89-L96 H1 H31-H35B H26-H35B H26-H32 H30-H35B (Kabat numbering) H1 H31-H35 H26-H35 H26-H32 H30-H35 (Chothia numbering) H2 H50-H65 H50-H58 H53-H55 H47-H58 H3 H95-H102 H95-H102 H96-H101 H93-H101 HVRs may comprise “extended HVRs” as follows: 24-36 or 24-34 (L1), 46-56 or 50-56 (L2), and 89-97 or 89-96 (L3) in the VL, and 26-35 (H1), 50-65 or 49-65 (a preferred embodiment) (H2), and 93-102, 94-102, or 95-102 (H3) in the VH. The variable-domain residues are numbered according to Kabat et al., supra, for each of these extended-HVR definitions. “Framework” or “FR” residues are those variable-domain residues other than the HVR residues as herein defined. An “acceptor human framework” as used herein is a framework comprising the amino acid sequence of a VL or VH framework derived from a human immunoglobulin framework or a human consensus framework. An acceptor human framework “derived from” a human immunoglobulin framework or a human consensus framework may comprise the same amino acid sequence thereof, or it may comprise pre-existing amino acid sequence changes. In some embodiments, the number of pre-existing amino acid changes are 10 or less, 9 or less, 8 or less, 7 or less, 6 or less, 5 or less, 4 or less, 3 or less, or 2 or less. Where pre-existing amino acid changes are present in a VH, preferable those changes occur at only three, two, or one of positions 71H, 73H and 78H; for instance, the amino acid residues at those positions may by 71A, 73T and/or 78A. In one embodiment, the VL acceptor human framework is identical in sequence to the VL human immunoglobulin framework sequence or human consensus framework sequence. A “human consensus framework” is a framework that represents the most commonly occurring amino acid residues in a selection of human immunoglobulin VL or VH framework sequences. Generally, the selection of human immunoglobulin VL or VH sequences is from a subgroup of variable domain sequences. Generally, the subgroup of sequences is a subgroup as in Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md. (1991). Examples include for the VL, the subgroup may be subgroup kappa I, kappa II, kappa III or kappa IV as in Kabat et al., supra. Additionally, for the VH, the subgroup may be subgroup I, subgroup II, or subgroup III as in Kabat et al., supra. An “amino-acid modification” at a specified position, e.g., of an anti-TMEM106B antibody of the present disclosure, refers to the substitution or deletion of the specified residue, or the insertion of at least one amino acid residue adjacent the specified residue. Insertion “adjacent” to a specified residue means insertion within one to two residues thereof. The insertion may be N-terminal or C-terminal to the specified residue. The preferred amino acid modification herein is a substitution. An “affinity-matured” antibody, such as an affinity matured anti-TMEM106B antibody of the present disclosure, is one with one or more alterations in one or more HVRs thereof that result in an improvement in the affinity of the antibody for antigen, compared to a parent antibody that does not possess those alteration(s). In one embodiment, an affinity-matured antibody has nanomolar or even picomolar affinities for the target antigen. Affinity-matured antibodies are produced by procedures known in the art. For example, Marks et al. Bio/Technology 10:779-783 (1992) describes affinity maturation by VH- and VL-domain shuffling. Random mutagenesis of HVR and/or framework residues is described by, for example: Barbas et al. Proc Nat. Acad. Sci. USA 91:3809-3813 (1994); Schier et al. Gene 169:147-155 (1995); Yelton et al. J. Immunol. 155: 1994-2004 (1995); Jackson et al. J Immunol. 154(7):3310-9 (1995); and Hawkins et al., J. Mol. Biol. 226:889-896 (1992). “Fv” is the minimum antibody fragment which comprises a complete antigen-recognition and -binding site. This fragment consists of a dimer of one heavy- and one light-chain variable region domain in tight, non-covalent association. From the folding of these two domains emanate six hypervariable loops (3 loops each from the H and L chain) that contribute the amino acid residues for antigen binding and confer antigen binding specificity to the antibody. However, even a single variable domain (or half of an Fv comprising only three HVRs specific for an antigen) has the ability to recognize and bind antigen, although at a lower affinity than the entire binding site. “Single-chain Fv” also abbreviated as “sFv” or “scFv” are antibody fragments that comprise the VH and VL antibody domains connected into a single polypeptide chain. Preferably, the sFv polypeptide further comprises a polypeptide linker between the VH and VL domains, which enables the sFv to form the desired structure for antigen binding. Antibody “effector functions” refer to those biological activities attributable to the Fc region (a native sequence Fc region or amino acid sequence variant Fc region) of an antibody, and vary with the antibody isotype. The term “Fc region” herein is used to define a C-terminal region of an immunoglobulin heavy chain, including native-sequence Fc regions and variant Fc regions. Although the boundaries of the Fc region of an immunoglobulin heavy chain might vary, the human IgG heavy-chain Fc region is usually defined to stretch from an amino acid residue at position Cys226, or from Pro230, to the carboxyl-terminus thereof. The C-terminal lysine (residue 447 according to the EU numbering system) of the Fc region may be removed, for example, during production or purification of the antibody, or by recombinantly engineering the nucleic acid encoding a heavy chain of the antibody. Accordingly, a composition of intact antibodies may comprise antibody populations with all K447 residues removed, antibody populations with no K447 residues removed, and antibody populations having a mixture of antibodies with and without the K447 residue.
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