SNAP 25 (SNAP25) Recombinant Protein

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. It is essential for regulated exocytosis in neuronal cells. Alternative transcript variants encoding two different protein isoforms have been described for this gene. [provided by RefSeq, Jul 2012]

SNAP-25: a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Part of the SNARE core complex containing SNAP25, VAMP2 and syntaxin 1A. Associates with proteins involved in vesicle docking and membrane fusion. Two alternatively spliced isoforms have been described.

Protein type: Vesicle

Cellular Component: voltage-gated potassium channel complex; neuron projection; cell; terminal button; intracellular organelle; trans-Golgi network; cytosol; lipid raft; actin cytoskeleton; SNARE complex; growth cone; membrane; cell soma; axon; lamellipodium; perinuclear region of cytoplasm; cytoplasm; plasma membrane; synapse; cell junction; myelin sheath; endosome; vesicle; filopodium

Molecular Function: protein domain specific binding; SNAP receptor activity; SNARE binding; voltage-gated potassium channel activity; protein binding; myosin binding; syntaxin-1 binding; protein N-terminus binding; calcium-dependent protein binding

Biological Process: exocytosis; neurotransmitter secretion; calcium ion-dependent exocytosis of neurotransmitter; positive regulation of hormone secretion; positive regulation of insulin secretion; endosome transport; sleep; synaptic vesicle fusion to presynaptic membrane; growth hormone secretion; axonogenesis; long-term memory; regulation of synaptogenesis; synaptic vesicle priming