| References |
| Formulation |
Antibody from clarified ascites containing 0.02% sodium azide |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
Background Reading
Blume-Jensen, P., and Hunter, T. Oncogenic kinase signalling. Nature 411 355-365 (2001).
Goto, H., Kiyono, T., Tomono, Y., et al. Complex formation of Plk1 and INCENP required for metaphase-anaphase transition. Nat Cell Biol 8 180-187 (2005).
Ross, A.H., Baltimore, D., and Eisen, H.N. Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten. Nature 294 654-656 (1981).
Frackelton, A.R., Ross, A.H., and Eisen, H.N. Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells. Mol Cell Biol 3(8) 1343-1352 (1983).
Pawson, T., and Saxton, T.M. Signaling networks - Do all roads lead to the same genes? Cell 97 675-678 (1999).
Downward, J. The ins and outs of signalling. Nature 411 759-762 (2001).
Ostrovsky, P.C., and Maloy, S. Protein phosphorylation on serine, threonine, and tyrosine residues modulates membrane-protein interactions and transcriptional regulation in Salmonella typhimurium. Genes Dev 9 2034-2041 (1995).
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| Size |
Global Purchasing |
| 100 µL |
|
Description
Clone designation:
13F9
·
Host:
mouse
·
Isotype:
IgG1κ
·
Application(s):
ELISA and WB
·
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 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.2,3,4In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity.5 Specific antibodies can detect phosphotyrosine and are therefore helpful for facilitating the identification of tyrosine kinase substrates in vivo.6
1
Goto, H., Kiyono, T., Tomono, Y., et al. Complex formation of Plk1 and INCENP required for metaphase-anaphase transition. Nat Cell Biol 8 180-187 (2005).
2
Blume-Jensen, P., and Hunter, T. Oncogenic kinase signalling. Nature 411 355-365 (2001).
3
Downward, J. The ins and outs of signalling. Nature 411 759-762 (2001).
4
Pawson, T., and Saxton, T.M. Signaling networks - Do all roads lead to the same genes? Cell 97 675-678 (1999).
5
Frackelton, A.R., Ross, A.H., and Eisen, H.N. Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells. Mol Cell Biol 3(8) 1343-1352 (1983).
6
Ross, A.H., Baltimore, D., and Eisen, H.N. Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten. Nature 294 654-656 (1981).
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