VAMP1 Recombinant Rabbit Monoclonal Antibody [JG40-19] (ET7109-03)

UNIPROT #

P23763

PROTEIN NAME

VAMP1

SYNONYMS

DKFZp686H12131 antibody;SYB 1 antibody;SYB1 antibody;Synaptobrevin 1 antibody;Synaptobrevin-1 antibody;Synaptobrevin1 antibody;VAMP 1 antibody;VAMP-1 antibody;Vamp1 antibody;VAMP1_HUMAN antibody;Vesicle associated membrane protein 1 antibody;Vesicle associated membrane protein 1 synaptobrevin 1 antibody;Vesicle-associated membrane protein 1 antibody

SEQUENCE SIMILARITIES

Belongs to the synaptobrevin family.

TISSUE SPECIFICITY

Nervous system, skeletal muscle and adipose tissue.

POST-TRANSLATIONAL MODIFICATION

(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which probably hydrolyzes the 78-Gln-|-Phe-79 bond and inhibits neurotransmitter release.; (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 61-Arg-|-Leu-62 bond and inhibits neurotransmitter release. BoNT/D has low catalytic activity on this protein due to its sequence. 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 probably hydrolyzes the 60-Gln-|-Lys-61 bond and inhibits neurotransmitter release.; (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which probably hydrolyzes the 68-Arg-|-Ala-69 bond and inhibits neurotransmitter release. It remains unknown whether BoNT/X is ever produced, or what organisms it targets.

SUBCELLULAR LOCATION

Mitochondrion. Synapse. Synaptosome.

FUNCTION

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. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined.