- 2 ug/mL (WB), 0.5 ug/mL (ELISA), 10 ug/mg (IP)
- Additional Information:
- Background Info: Recognizes proteins phosphorylated on threonine residues. Does not cross-react with phosphotyrosine.
- Scientific 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).
- Certificate of Analysis: 2ug/mL was sufficient for detection of phosphorylation signal in western blot analysis using mouse spleen extract treated with Vanadium.
- Target Reference:
- 1. Goto H. et al. (2005). Nature Cell Biology 8: 180-187. 2. Blume-Jensen P. and Hunter T. (2001). Nature 411: 355-
3. Downward J. (2001). Nature 411: 759-762.
4. Pawson T. and Saxton T.M. (1999). Cell 97: 675-678.
5. Ostrovsky PC. (1995). Genes Dev. 9(16): 2034-2041.
- Storage Buffer:
- PBS, 50% glycerol, 0.09% sodium azide