Lane 1: Mouse cerebellum
Lane 2: Rat brain
Recombinant Rabbit monoclonal primary
VAMP1 Recombinant Rabbit Monoclonal Antibody [JG40-19] (ET7109-03)
Full length recombinant protein of human vamp1.
Mouse cerebellum tissue, rat brain tissue, 293T, Hela, SH-SY-5Y, human prostate cancer tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
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
Belongs to the synaptobrevin family.
Nervous system, skeletal muscle and adipose tissue.
(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.
Mitochondrion. Synapse. Synaptosome.
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.