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SNAP25 Polyclonal antibody, PBS Only

SNAP25 Polyclonal Antibody for WB, IF/ICC, IP, Indirect ELISA

Host / Isotype

Rabbit / IgG

Reactivity

human, mouse, rat

Applications

WB, IF/ICC, IP, Indirect ELISA

Conjugate

Unconjugated

Cat no : 14903-1-PBS

Synonyms



Product Information

14903-1-PBS targets SNAP25 in WB, IF/ICC, IP, Indirect ELISA applications and shows reactivity with human, mouse, rat samples.

Tested Reactivity human, mouse, rat
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen SNAP25 fusion protein Ag6695
Full Name synaptosomal-associated protein, 25kDa
Calculated Molecular Weight 23 kDa
Observed Molecular Weight 25-27 kDa
GenBank Accession NumberBC010647
Gene Symbol SNAP25
Gene ID (NCBI) 6616
Conjugate Unconjugated
Form Liquid
Purification MethodAntigen affinity purification
Storage Buffer PBS Only
Storage ConditionsStore at -80°C.

Background Information

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 AX type E can be rescued by a SNAP-25 C-terminal peptide, probably by initiating the formation of a fusion competent SNARE complex.