SNAP23 (NM_003825) Human Mass Spec Standard

CAT#: PH301596

SNAP23 MS Standard C13 and N15-labeled recombinant protein (NP_003816)



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CNY 19,520.00


货期*
4周

规格
    • 10 ug

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Specifications

Product Data
Description SNAP23 MS Standard C13 and N15-labeled recombinant protein (NP_003816)
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC201596
Predicted MW 23.4 kDa
Protein Sequence
Tag C-Myc/DDK
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration >0.05 µg/µL as determined by microplate BCA method
Labeling Method Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Buffer 25 mM Tris-HCl, 100 mM glycine, pH 7.3
Reference Data
RefSeq NP_003816
RefSeq Size 2650
RefSeq ORF 633
Synonyms HsT17016; SNAP-23; SNAP23A; SNAP23B
Locus ID 8773
Cytogenetics 15q15.1-q15.2
Summary 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 transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq, Jul 2008]
Protein Families Druggable Genome
Protein Pathways SNARE interactions in vesicular transport
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