|Application ||WB, IP, ICC/IF|
|Description||Rabbit Anti-Phosphothreonine Polyclonal|
|Target/Specificity||Detects proteins phosphorylated on threonine residues. Does not cross-react with phosphotyrosine.|
|Other Names||Phospho-threonine Antibody|
|Immunogen||Phosphothreonine conjugated to KLH|
|Purification||Protein A Purified|
|Storage Buffer||PBS, 50% glycerol, 0.09% sodium azide|
|Shipping Temperature||Blue Ice or 4ºC|
|Certificate of Analysis||2 µg/ml of SPC-154 was sufficient for detection of phosphorylation signal in western blot analysis using mouse spleen extract treated with Vanadium.|
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Provided below are standard protocols that you may find useful for product applications.
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).
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. Ostrovsky P.C. (1995) Genes Dev. 9(16): 2034-2041.
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