Phosphotyrosine (HRP)

Protein phosphorylation is an important post-translational 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).\n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher. \n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

P4075-29C

Size

400ul

Applications

WB

Hosts

Rabbit

Form

Supplied as a liquid in TBS, 0.01% preservative. Labeled with horseradish peroxidasae (HRP).

P Type

Pab

Purity

Purified

Isotype

IgG

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.

Additional Info

Recognizes proteins and peptides that contain phosphorylated tyrosine residues. Does not crossreact with phosphoserine or threonine.