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alpha SNAP antibody

Catalog Number:

22791
other_names:

Amount:

100μg
calculated_mw:
host_species: Rabbit

Price:

$319

Swiss-Prot No:

Swiss-Prot:P54920
Gene ID:8775

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:

appl_detail:

Predicted MW: 33kd
Western blotting: 1:500-1:3000
Immunofluorescence: 1:100-1:200

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