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Recombinant human SNAP23 protein

Cat:P08450

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 1-200aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: SNAP23
【Full Name】: synaptosomal-associated protein,23kDa
【Uniprot】: O00161
【Gene ID】: 8773
【Species Reactivity】: Human Mouse Rat
【Mol Mass】: 22.2kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: No activity experimental data, to be verified.
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 10μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 2-7 days, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues. The protein encoded by this gene is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion. Two alternative transc

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