SNAP25 antibody

SNAP25 antibody

• DataSheet
• Material Safety Data Sheets (MSDS)

SNAP25 Mouse Monoclonal antibody. Positive WB detected in fetal human brain tissue, HEK-293 cells. Positive IP detected in mouse brain tissue. Positive IF detected in PC-12 cells. Observed molecular weight by Western-blot: 28-32 kDa

ELISA, IF, IP, WB

Human, Mouse, Rat; other species not tested.

bA416N4.2 antibody; dJ1068F16.2 antibody; FLJ23079 antibody; RIC 4 antibody; RIC4 antibody; SEC9 antibody; SNAP antibody; SNAP 25 antibody; SNAP25 antibody; SUP antibody; Super protein antibody

Mouse IgG2b

This antibody was obtained by immunization of SNAP25 recombinant protein (Accession Number: XM_017028022). Purification method: Caprylic acid/ammonium sulfate precipitation.

Monoclonal

PBS with 0.1% sodium azide and 50% glycerol pH 7.3.

Store at -20℃. DO NOT ALIQUOT

The synaptosomal associated protein of 25 kD (SNAP-25) was first identified as a major synaptic protein by Wilson and colleagues. The protein interacts with syntaxin and synaptobrevin through its N-terminal and C-terminal -helical domains. Its palmitoylation domain is located in the middle of the molecule that contains four cysteine residues. Mutation of the cysteines abolishes palmitoylation and membrane binding. Several elegant studies using synaptosome preparations and permeabilized PC12 cells have suggested that SNAP-25 may act in the late post-docking steps of exocytosis. By limited proteolysis and in vitro binding assay, it is proposed that the two helix domains act independently and contribute equally to form the SNARE complex with syntaxin and synaptobrevin. It seems that a major regulatory element is located in the C-terminus of SNAP-25. Removing a 9 amino acid sequence of SNAP-25 inhibited neurosecretion in chromaffin cells. In addition, it has been shown that inhibition of neurosecretion by botulinum toxin E can be rescued by a SNAP-25 C-terminal peptide, probably by initiating the formation of a fusion competent SNARE complex.