Human SNAP25 / SUP Protein (His Tag)
bA416N4.2,dJ1068F16.2,RIC-4,RIC4,SEC9,SNAP,SNAP-25
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| Catalog Number | P11585-H07E |
|---|---|
| Organism Species | Human |
| Host | E. coli |
| Synonyms | bA416N4.2,dJ1068F16.2,RIC-4,RIC4,SEC9,SNAP,SNAP-25 |
| Molecular Weight | The recombinant human SNAP25 consisting of 217 amino acids and has a calculated molecular mass of 24.8 kDa. It migrates as an approximately 28 kDa band in SDS-PAGE under reducing conditions. |
| predicted N | Met |
| SDS-PAGE |  |
| Purity | > 90 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the human SNAP25 (P60880-1) (Met 1-Gly 206) was expressed, with a polyhistide tag at the N-terminus. |
| Bio-activity | |
| Research Area | Signaling |Signal Transduction |Metabolism |Types of disease |Metabolism in Cancer |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | Synaptosomal-associated protein 25, also known as Super protein, Synaptosomal-associated 25 kDa protein, SNAP25 and SNAP, is a cytoplasm and cell membrane protein which belongs to the SNAP-25 family. SNAP25 / SUP contains 2 t-SNARE coiled-coil homology domains. SNAP25 / SUP is a membrane bound protein anchored to the cytosolic face of membranes via palmitoyl side chains in the middle of the molecule. SNAP25 / SUP protein is a component of the SNARE complex, which is proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP25 / SUP is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin. SNAP25 / SUP is involved in the molecular regulation of neurotransmitter release. It may play an important role in the synaptic function of specific neuronal systems. SNAP25 / SUP associates with proteins involved in vesicle docking and membrane fusion. SNAP25 / SUP regulates plasma membrane recycling through its interaction with CENPF. SNAP25 / SUP inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion. In glutamatergic synapses SNAP25 / SUP decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses. |
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