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Description
Release of neurotransmitters from neurons is regulated by exocytosis of synaptic vesicles. This exocytosis is mediated by a complex consisting of membrane components of both the synaptic vesicle and the synaptic plasma membrane. The fusion complex consists of the soluble NSF (N-ethyl-maleimide-sensitive factor) and SNAPs (soluble NSF attachment proteins), along with the receptor proteins (known as SNAREs) synaptobrevin, synaptotagmin, syntaxin, and SNAP-25 (synaptosomal-associated protein of 25kDa- the name is coincidental to the previously mentioned “SNAP” terminology). SNAP-25 and syntaxin are plasmalemmal proteins (designated as t-SNAREs) while synaptobrevin and synaptotagmin are vesicular proteins (designated as v-SNAREs). These four proteins are thought to constitute an initial SNARE docking complex for regulated exocytosis. SNAP-25 lacks a transmembrane domain, but is linked to the membrane by palmitoylated cysteine residues in the central region of the molecule.
Immunofluorescence, Immunoprecipitation, Western Blotting
Specifications
Specifications
| Antigen | SNAP-25 |
| Applications | Immunofluorescence, Western Blot |
| Classification | Monoclonal |
| Clone | 20 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Description | Synaptosomal Associated Protein of 25 kD |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
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Safety and Handling
For Research Use Only.
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