VAP-B/C Antibody (1A2): sc-293364

VAP-B/C Antibody (1A2) is a mouse monoclonal IgG2b kappa light chain antibody that detects VAP-B/C protein of human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-VAP-B/C antibody (1A2) is available as the non-conjugated format. VAP-B protein, consisting of 243 amino acids, plays a crucial role in regulating SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) proteins, which are essential for membrane fusion and intracellular transport. VAP-B includes a conserved N-terminal domain, an alpha-helical coiled-coil domain, and a C-terminal transmembrane domain, all vital for interaction with SNAREs and other proteins involved in vesicular transport. VAP-C, a splice variant of VAP-B, is shorter at 99 amino acids and retains the N-terminal 70 residues but lacks the coiled-coil and transmembrane domains, highlighting the importance of structural integrity in protein function. Mutations in VAP-B/C gene have been linked to severe neurodegenerative disorders, including amyotrophic lateral sclerosis and spinal muscular atrophy, underscoring VAP-B/C′s significance in maintaining neuronal health and function.

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VAP-B/C Antibody (1A2) References:

1. Velvet antler polypeptides promoted proliferation of chondrocytes and osteoblast precursors and fracture healing.  |  Zhou, QL., et al. 1999. Zhongguo Yao Li Xue Bao. 20: 279-82. PMID: 10452108
2. VAP-A binds promiscuously to both v- and tSNAREs.  |  Weir, ML., et al. 2001. Biochem Biophys Res Commun. 286: 616-21. PMID: 11511104
3. A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis.  |  Nishimura, AL., et al. 2004. Am J Hum Genet. 75: 822-31. PMID: 15372378
4. Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction.  |  Amarilio, R., et al. 2005. J Biol Chem. 280: 5934-44. PMID: 15545272
5. Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B.  |  Hamamoto, I., et al. 2005. J Virol. 79: 13473-82. PMID: 16227268
6. A VAMP-binding protein from Aplysia required for neurotransmitter release.  |  Skehel, PA., et al. 1995. Science. 269: 1580-3. PMID: 7667638
7. Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues.  |  Ravichandran, V., et al. 1996. J Biol Chem. 271: 13300-3. PMID: 8663154
8. Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins.  |  Nishimura, Y., et al. 1999. Biochem Biophys Res Commun. 254: 21-6. PMID: 9920726