Rabbit anti-Phosphotyrosine - SPC-162F
|Product Name ||Phosophotyrosine Antibody:HRP|
|Catalog # ||SPC-162F|
|Package size ||400ul|
|Datasheet ||SPC 162 Phosphotyrosine HRP Cell Signaling|
|Description ||HRP Anti-Phosphotyrosine|
|Research Area ||Cell Signaling, Phosphorylation, Post-translational Modifications|
|Alternative Names ||N/A|
|Clone Number ||N/A|
|Host Species ||Rabbit|
|Immunogen ||Phosphotyrosine conjugated to KLH|
|Species Reactivity ||Proteins and peptides that contain phosphorylated tyrosine residues|
|Accession Number ||N/A|
|Background Info ||Recognizes proteins phosphorylated on tyrosine residues. Does not cross-react with phosphoserine or threonine.|
|Form ||Affinity Purified, HRP conjugated|
|Storage Buffer ||PBS, 50% glycerol, 0.09% sodium azide|
|Storage Temp ||-20 °C|
|Shipping Temp ||Blue Ice or 4 °C|
|Research Background ||Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein’s activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine; others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time (1). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders (2-4). In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity (5). Phosphotyrosine can be detected through specific antibodies, and are helpful in facilitating the identification of tyrosine kinase substrates (6).|
|References ||1. Goto, H. et al. (2005). Nature Cell Biology 8: 180-187.|
2. Blume-Jensen, P. and Hunter, T. (2001). Nature 411: 355-365.
3. Downward, J. (2001). Nature 411: 759-762.
4. Pawson, T. and Saxton, T.M. (1999). Cell 97: 675-678.
5. Frackelton, A.R. Jr., Ross, A.H., and Eisen, H.N. (1983). Mol Cell Biol. 3: 1343-1352.
6. Ross, A.H., Baltimore, D., and Eisen, H.N. (1981). Nature 294: 654-656.
7. Ostrovsky, PC. (1995). Genes Dev. 9(16): 2034-2041.