Cellubrevin Recombinant Rabbit Monoclonal Antibody [JG36-31] (ET7108-31)

UNIPROT #

Q15836

PROTEIN NAME

Cellubrevin

SYNONYMS

CEB antibody;Cellubrevin antibody;Synaptobrevin 3 antibody;Synaptobrevin-3 antibody;VAMP 3 antibody;VAMP-3 antibody;VAMP3 antibody;VAMP3_HUMAN antibody;Vesicle associated membrane protein 3 antibody;Vesicle-associated membrane protein 3 antibody

SEQUENCE SIMILARITIES

Belongs to the synaptobrevin family.

POST-TRANSLATIONAL MODIFICATION

(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 59-Gln-|-Phe-60 bond and probably inhibits neurotransmitter release.; (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which hydrolyzes the 42-Lys-|-Leu-43 bond and probably inhibits neurotransmitter release. Note that humans are not known to be infected by C.botulinum type D.; (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which hydrolyzes the 41-Gln-|-Lys-42 bond and probably inhibits neurotransmitter release.

SUBCELLULAR LOCATION

Membrane.

FUNCTION

Vesicle-associated membrane proteins, known as VAMPs, also designated synaptobrevins, include VAMP-1, VAMP-2, VAMP-3 (cellubrevin), and synaptotagmin, a protein that may function as an inhibitor of exocytosis. VAMP proteins are vesicular factors that are important components of the machinery controlling docking and/or fusion of secretory vesicles with their target membrane. Synaptosomal-associated proteins, known as SNAPs, including alpha- and gamma-SNAP, are cytoplasmic proteins that bind to a membrane receptor complex composed of VAMP, SNAP 25 and syntaxin. Pancreatic beta-cells express VAMP-2 and VAMP-3, and either one or both of these proteins selectively control Ca2+-mediated insulin secretion. In addition, VAMP-2 and VAMP-3 are expressed on GLUT4-containing vesicle membranes isolated from 3T3-Ll adipocytes and are important components of the insulin-dependent translocation of GLUT4 to the cell surface in adipocytes.