VAMP-1/2 Antibody (SP10): sc-20039

VAMP-1/2 Antibody (SP10) is a mouse monoclonal IgM antibody that detects VAMP-1/2 protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). Anti-VAMP-1/2 antibody (SP10) is available as a non-conjugated format. VAMP-1 and VAMP-2 proteins, also known as synaptobrevins, play a crucial role in synaptic vesicle exocytosis, which is essential for neurotransmitter release in the nervous system. VAMP-1/2 (SP10) antibody targets proteins located on the vesicular membrane that interact with syntaxins and SNAPs to facilitate synaptic vesicle fusion with the plasma membrane, enabling neurotransmitter release into the synaptic cleft. This process is vital for proper neuronal communication and function, and dysregulation of VAMP proteins can lead to various neurological disorders. VAMP-1 and VAMP-2 are also involved in other cellular processes, including protein and lipid transport within cells, highlighting their importance beyond synaptic transmission. Anti-VAMP-1/2 antibody (SP10) effectively detects these proteins, making this reagent an invaluable tool for researchers studying synaptic function and related pathologies.

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VAMP-1/2 Antibody (SP10) References:

1. VAMP-1, VAMP-2, and syntaxin-4 regulate ANP release from cardiac myocytes.  |  Ferlito, M., et al. 2010. J Mol Cell Cardiol. 49: 791-800. PMID: 20801128
2. Distribution of SNAP25, VAMP1 and VAMP2 in mature and developing deep cerebellar nuclei after estrogen administration.  |  Manca, P., et al. 2014. Neuroscience. 266: 102-15. PMID: 24534378
3. Calcineurin/NFAT signaling represses genes Vamp1 and Vamp2 via PMCA-dependent mechanism during dopamine secretion by Pheochromocytoma cells.  |  Kosiorek, M., et al. 2014. PLoS One. 9: e92176. PMID: 24667359
4. The syntaxin family of vesicular transport receptors.  |  Bennett, MK., et al. 1993. Cell. 74: 863-73. PMID: 7690687
5. Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine.  |  Edelmann, L., et al. 1995. EMBO J. 14: 224-31. PMID: 7835333
6. Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity alpha-SNAP binding site.  |  McMahon, HT. and Südhof, TC. 1995. J Biol Chem. 270: 2213-7. PMID: 7836452
7. Exocytosis relating proteins in the nervous system.  |  Yamaguchi, K. and Akagawa, K. 1994. Neurosci Res. 20: 289-92. PMID: 7870381
8. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly.  |  Hayashi, T., et al. 1994. EMBO J. 13: 5051-61. PMID: 7957071
9. A role for synaptotagmin (p65) in regulated exocytosis.  |  Elferink, LA., et al. 1993. Cell. 72: 153-9. PMID: 8422678
10. Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis.  |  Barnard, RJ., et al. 1997. J Cell Biol. 139: 875-83. PMID: 9362506
11. Structural organization of the synaptic exocytosis core complex.  |  Lin, RC. and Scheller, RH. 1997. Neuron. 19: 1087-94. PMID: 9390521
12. VAMP-1 and VAMP-2 gene expression in rat spinal motoneurones: differential regulation after neuronal injury.  |  Jacobsson, G., et al. 1998. Eur J Neurosci. 10: 301-16. PMID: 9753139

The preferred VAMP-2 antibody is VAMP-2 Antibody (3E5): sc-69706.