Synaptobrevin antibody [SP10]

Application	Recommended Dilution
WB	Assay dependent
IHC	Assay dependent

16 kDa. ( Note )

Liquid

10mM HEPES, 150mM NaCl, 0.01% BSA, 50% Glycerol

No preservative

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

Batch dependent (Please refer to the vial label for the specific concentration.)

Human

Synaptic immunoprecipitate (crude) from human brain

IgM Purified

For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.

Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.

VAMP1/2 , SYB1 , VAMP1 , VAMP-1 , DKFZp686H12131 , VAMP 1

Vesicle-associated membrane protein (VAMP), also known as synaptobrevin, is an 18kD integral membrane protein localized to the cytoplasmic surface of synaptic vesicle. VAMP consists of a proline-rich amino-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a carboxyl-terminal tail. Two VAMP homologs, VAMP1 and VAMP2, are differentially expressed in the nervous system. VAMP1 expression is localized to neurons involved in modulating overlapping patterns, whereas VAMP2 is found in neurons associated with autonomic, sensory and integrative functions. In non-neuronal tissues, VAMP1 is restricted to pancreas and kidney tubular cells, whereas VAMP2 is predominantly expressed in Langerhans islets and glomerular cells. Evidences for VAMP’s involvement in vesicular transport and neurotransmission include the requirement of its yeast homologs, SNC 1 and 2, in targeting and fusion of Golgi- derived vesicles with the plasma membrane. VAMP is also the target of clostridial neurotoxins that block neurotransmitter release from presynaptic terminals. VAMP is a component of a 20S complex implicated in vesicle docking and fusion. The formation of 20S complex involves the interaction of VAMP with syntaxin through an ATP-dependent reaction modulated by synaptotagmin, SNAP-25, alpha-SNAP, and NSF.