catalog number :
MBS635835
products type :
Recombinant Protein
products full name :
VAMP 2, Recombinant, Human (Synaptobrevin 2, Vehicle-associated membrane)
products short name :
[VAMP 2]
other names :
[vesicle-associated membrane protein 2; Vesicle-associated membrane protein 2; vesicle-associated membrane protein 2; VAMP-2; synaptobrevin-2; vesicle-associated membrane protein 2 (synaptobrevin 2); Synaptobrevin-2]
other gene names :
[VAMP2; VAMP2; SYB2; VAMP-2]
uniprot entry name :
VAMP2_BOVIN
sequence :
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA TAATAPPAAP AGEGGPPAPP PNLTSNRRLQ QTQAQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG ASQFETSAAK
purity :
Highly Purified. 95% by SDS PAGE
form :
Supplied as a liquid in PBS, pH 7.4, 1mM EDTA
storage stability :
For long-term storage, store at -20 degree C. Aliquots are stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
app notes :
Suitable for use in Western Blot. Optimal dilutions to be determined by the researcher.
image1 heading :
SDS-Page
products categories :
Molecular Biology; MB-Proteins
products description :
Synaptobrevin 2 (Vehicle-associated membrane, VAMP2), which is an 18kD integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25. Recombinant protein corresponding to aa1-89 of human VAMP 2, His- tag expressed in E. coli (NP_055047).
ncbi acc num :
NP_776908.1
ncbi gb acc num :
NM_174483.2
ncbi pathways :
Acetylcholine Neurotransmitter Release Cycle Pathway (827808); Clathrin Derived Vesicle Budding Pathway (827612); GABA Synthesis, Release, Reuptake And Degradation Pathway (827809); Glutamate Neurotransmitter Release Cycle Pathway (827806); Insulin Secretion Pathway (777536); Integration Of Energy Metabolism Pathway (827468); Membrane Trafficking Pathway (827608); Metabolism Pathway (827337); Neuronal System Pathway (827798); Neurotransmitter Release Cycle Pathway (827803)
uniprot summary :
VAMP2: a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. 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. Protein type: Membrane protein, integral; Vesicle; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 17p13.1. Cellular Component: neuron projection; zymogen granule membrane; synaptic vesicle membrane; intracellular membrane-bound organelle; clathrin-coated vesicle; secretory granule membrane; integral to plasma membrane; trans-Golgi network; cytosol; secretory granule; SNARE complex; synaptic vesicle; membrane; perinuclear region of cytoplasm; plasma membrane; synapse; cytoplasmic vesicle; cell junction. Molecular Function: calmodulin binding; SNAP receptor activity; protein binding; SNARE binding; protein self-association; syntaxin binding; syntaxin-1 binding; phospholipid binding; calcium-dependent protein binding. Biological Process: exocytosis; natural killer cell degranulation; neurotransmitter secretion; neutrophil degranulation; pathogenesis; calcium ion-dependent exocytosis; vesicle-mediated transport; regulation of exocytosis; vesicle fusion; synaptic transmission; protein transport; synaptic vesicle exocytosis; cellular protein metabolic process; cellular response to insulin stimulus; glutamate secretion; Golgi to plasma membrane protein transport; response to glucose stimulus; energy reserve metabolic process; eosinophil degranulation; protein complex assembly; post-Golgi vesicle-mediated transport; regulation of insulin secretion