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Vesicle-Associated Membrane Protein 2 (Synaptobrevin 2) (VAMP2) antibody
|Synonyms||SYB2, VAMP-2, FLJ11460, Syb2, Syb-2, SYB, RATVAMPB, RATVAMPIR, zgc:73302, wu:fj61c06, VAMP2, vamp2-b, xsybii, MGC68783, MGC154285, vamp2-a, xsybi|
Alternatives Immunohistochemistry (IHC), Western Blotting (WB)
|7 references available|
|Quantity||100 µl (Variants)|
|Price||454.67 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 7 to 8 Business Days|
|Alternative name||Vesicle-associated membrane protein 2 (VAMP-2, Synaptobrevin-2, VAMP2, SYB2)|
|Immunogen||A synthetic peptide from human Vesicle-associated membrane protein 2 (VAMP-2, Synaptobrevin-2, VAMP2, SYB2) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in many other species including rat, mouse and xenopus.|
|Description||The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated proteinSNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. It is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG. FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell junction, synapse, synaptosome. Note: Neuronal synaptic vesicles. Also known as: VAMP-2, Synaptobrevin-2, VAMP2, SYB2.|
|Specificity||Appears to be specific for VAMP2.|
|Application Notes||IHC, WB. A dilution of 1 : 300 to 1 : 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.|
|Storage||Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.|
|Restrictions||For Research Use only|
Archer, Ozucelik, Jahn et al.: "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2." in: The Journal of biological chemistry, Vol. 265, Issue 28, pp. 17267-73, 1990 (PubMed).
Elferink, Trimble, Scheller: "Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system." in: The Journal of biological chemistry, Vol. 264, Issue 19, pp. 11061-4, 1989 (PubMed).
Kutay, Ahnert-Hilger, Hartmann et al.: "Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane." in: The EMBO journal, Vol. 14, Issue 2, pp. 217-23, 1995 (PubMed).
Jagadish, Fernandez, Hewish et al.: "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2." in: The Biochemical journal, Vol. 317 ( Pt 3), pp. 945-54, 1996 (PubMed).
Martin, Shewan, Millar et al.: "Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes." in: The Journal of biological chemistry, Vol. 273, Issue 3, pp. 1444-52, 1998 (PubMed).
Sutton, Fasshauer, Jahn et al.: "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution." in: Nature, Vol. 395, Issue 6700, pp. 347-53, 1998 (PubMed).
Hanson, Stevens: "Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution." in: Nature structural biology, Vol. 7, Issue 8, pp. 687-92, 2000 (PubMed).