SNAP-25 (Cleaved & Uncleaved) (SNAP25) Antibody – Mouse Monoclonal

Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq]

Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.

Subunit structure: Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with CENPF, TRIM9, RIMS1, SNAPIN, OTOF and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8. Found in a complex containing SYT1, SV2B and syntaxin-1

Subcellular location: Cytoplasm › perinuclear region

By similarity. Cell membrane; Lipid-anchor. Cell junction › synapse › synaptosome. Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region

Tissue specificity: Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum.

Post-translational modification: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association

Miscellaneous: When cloned and expressed in Eschericia coli, where protein palmitoylation does not occur, Cys-85, Cys-88, Cys-90 and Cys-92 in the protein sequence readily form an iron-sulfur cluster instead.

Sequence similarities: Belongs to the SNAP-25 family.Contains 2 t-SNARE coiled-coil homology domains.