1-832-868-1888
order@swbio.com
Catalog Number: |
22791 |
other_names: | |
Amount: |
100μg |
calculated_mw: | |
host_species: | Rabbit |
Price: |
$319 |
Swiss-Prot No: |
Swiss-Prot:P54920 |
Form of Antibody: |
Supplied in 0.1M Tris-buffered saline with 10% Glycerol (pH7.0). 0.01% Thimerosal was added as a preservative. |
Storage/Stability: |
|
Immunogen: |
Recombinant protein fragment contain a sequence corresponding to a region within amino acids 78 and 269 of Human NAPA |
Purification: |
Purified by antigen-affinity chromatography. |
Specificity/Sensitivity: |
|
Applications: |
WB IF |
Background: |
The 'SNARE hypothesis' is a model explaining the process of docking and fusion of vesicles to their target membranes. According to this model, membrane proteins from the vesicle (v-SNAREs) and proteins from the target membrane (t-SNAREs) govern the specificity of vesicle targeting and docking through mutual recognition. Once the 2 classes of SNAREs bind to each other, they form a complex that recruits the general elements of the fusion apparatus, namely NSF (N-ethylmaleimide-sensitive factor) and SNAPs (soluble NSF-attachment proteins), to the site of membrane fusion, thereby forming the 20S fusion complex. Alpha- and gamma-SNAP are found in a wide range of tissues and act synergistically in intra-Golgi transport. The sequence of the predicted 295-amino acid human protein encoded by NAPA shares 37%, 60%, and 67% identity with the sequences of yeast, Drosophila, and squid alpha-SNAP, respectively. Platelets contain some of the same proteins, including NSF, p115/TAP, alpha-SNAP, gamma-SNAP, and the t-SNAREs syntaxin-2 and syntaxin-4, that are used in many vesicular transport processes in other cell types. Platelet exocytosis uses a molecular mechanism similar to that used by other secretory cells, such as neurons, although the proteins used by the platelet and their modes of regulation may be quite different. [provided by RefSeq] |
References: |
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appl_detail: |
Predicted MW: 33kd |
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