VAMP7 Antibody #13920
Inquiry Info. # 13920
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Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 25 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
VAMP7 recognizes endogenous levels of total VAMP7 protein. This antibody cross-reacts with a protein of unknown origin at approximately 70 kDa.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala34 of human VAMP7 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion that pair vesicular SNAREs (v-SNAREs) with cognate target SNARE (t-SNARE) proteins (reviewed in 1,2). Vesicle-associated membrane protein 7 (VAMP7), or tetanus neurotoxin-insensitive VAMP (TI-VAMP), is a widely expressed v-SNARE involved in exocytosis of granules and synaptic vesicles in various cell types, membrane remodeling, neurite outgrowth, lysosomal secretion, and autophagosome maturation (3). Activity of VAMP7 can be regulated by c-Src-mediated tyrosine phosphorylation, which activates VAMP7-mediated exocytosis (4). VAMP7 activity can also be regulated through interaction with the guanine nucleotide exchange factor Varp (5,6). Several research studies indicate that VAMP7 plays an important role in neurite outgrowth as well as potential neurological activities, including anxiety (7-9). VAMP7 also appears to have a key role in T-cell activation by facilitating the recruitment of vesicular Lat to the immunological synapse (10). The VAMP7 protein interacts with ATG16L, a component of the ATG5-ATG12 complex, and regulates autophagosome maturation through homotypic fusion of ATG16L1 vesicles (11).
- Jena, B.P. (2011) Adv Exp Med Biol 713, 13-32.
- Kasai, H. et al. (2012) Physiol Rev 92, 1915-64.
- Galli, T. et al. (1998) Mol Biol Cell 9, 1437-48.
- Burgo, A. et al. (2013) J Biol Chem 288, 11960-72.
- Burgo, A. et al. (2012) Dev Cell 23, 166-80.
- Schäfer, I.B. et al. (2012) Nat Struct Mol Biol 19, 1300-9.
- Martinez-Arca, S. et al. (2000) J Cell Biol 149, 889-900.
- Alberts, P. et al. (2003) Mol Biol Cell 14, 4207-20.
- Danglot, L. et al. (2012) J Neurosci 32, 1962-8.
- Larghi, P. et al. (2013) Nat Immunol 14, 723-31.
- Moreau, K. et al. (2011) Cell 146, 303-17.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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