Phosphothreonine (Ascites) Monoclonal Antibody (Clone 18F6)

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.^2,3,4

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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).