VAMP-3 Antibody (k2A2): sc-136162
- VAMP-3 Antibody (k2A2) is a mouse monoclonal IgG2b, cited in 1 publications, provided at 50 µg/0.5 ml
- raised against a recombinant protein corresponding to amino acids 1-77 of VAMP-3 of human origin
- recommended for detection of VAMP-3 of mouse, rat and human origin by WB, IP and ELISA
- At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for VAMP-3 Antibody (k2A2). This work is in progress.
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VAMP-3 Antibody (k2A2) is a mouse monoclonal IgG2b antibody that detects VAMP-3 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). VAMP-3, also known as cellubrevin, plays a crucial role in the regulation of vesicle trafficking and exocytosis, which is essential for various cellular processes, including neurotransmitter release and hormone secretion. VAMP-3 is primarily located in the membranes of secretory vesicles, where VAMP-3 participates in the docking and fusion of these vesicles with target membranes, a process vital for proper synaptic transmission and insulin secretion in pancreatic beta-cells. VAMP-3 interacts with other proteins, such as synaptosomal-associated proteins (SNAPs) and syntaxin, forming a complex critical for precise regulation of vesicle fusion, ensuring neurotransmitters and hormones are released in a controlled manner. Anti-VAMP-3 antibody (k2A2) enables researchers to gain valuable insights into the mechanisms of vesicle-mediated transport and implications in various physiological and pathological conditions.
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VAMP-3 Antibody (k2A2) References:
- Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion. | Polgár, J., et al. 2002. Blood. 100: 1081-3. PMID: 12130530
- Vesicle associated membrane protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required for activation-induced degranulation of mature human mast cells. | Sander, LE., et al. 2008. Eur J Immunol. 38: 855-63. PMID: 18253931
- Transport of the major myelin proteolipid protein is directed by VAMP3 and VAMP7. | Feldmann, A., et al. 2011. J Neurosci. 31: 5659-72. PMID: 21490207
- miR-124/VAMP3 is a novel therapeutic target for mitigation of surgical trauma-induced microglial activation. | Chen, Y., et al. 2019. Signal Transduct Target Ther. 4: 27. PMID: 31637007
- Eukaryotic SNARE VAMP3 Dynamically Interacts with Multiple Chlamydial Inclusion Membrane Proteins. | Bui, DC., et al. 2021. Infect Immun. 89: PMID: 33229367
- Endocytic BDNF secretion regulated by Vamp3 in astrocytes. | Han, J., et al. 2021. Sci Rep. 11: 21203. PMID: 34707216
- Multifunctional regulation of VAMP3 in exocytic and endocytic pathways of RBL-2H3 cells. | Mishima, S., et al. 2022. Front Immunol. 13: 885868. PMID: 35990647
- Galectin-9 interacts with Vamp-3 to regulate cytokine secretion in dendritic cells. | Santalla Méndez, R., et al. 2023. Cell Mol Life Sci. 80: 306. PMID: 37755527
- miR-124 and VAMP3 Act Antagonistically in Human Neuroblastoma. | Zhang, X., et al. 2023. Int J Mol Sci. 24: PMID: 37834325
- Myeloid Vamp3 deletion attenuates CFA-induced inflammation and pain in mice via ameliorating macrophage infiltration and inflammatory cytokine production. | Dai, X., et al. 2023. Front Immunol. 14: 1239592. PMID: 37965323
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
VAMP-3 Antibody (k2A2) | sc-136162 | 50 µg/0.5 ml | $316.00 |