Antibodies for the analysis of kinases
Molecular model of the MEK kinase inhibitor drug Trametinib, which is used for the treatment of metastatic melanoma.
During a phosphorylation event, a phosphate group becomes added by a kinase to a serine, threonine or tyrosine residue of a target protein or substrate. This process can be reversed by another group of enzymes called phosphatases . Both kinases and phosphatases are specific with regards to whether they are phosphorylating or dephosphorylating tyrosine or serine/threonine residues.
Phosphorylation is a tightly regulated and fairly ubiquitous cellular process (according to Onclive.com “Today, it is believed that as many as one-third of all proteins in the cell are phosphorylated at one time or another, and half of these proteins likely harbor more than 1 phosphorylation site, with different sites often eliciting quite different cellular responses.” (De Lartigue J 2011)).
The process is also critical as aberrant phosphorylation levels and misregulation of phosphorylation cascades have been implicated in a variety of diseases, including cancer. Due to this correlation, much focus has recently been placed on developing specific kinase inhibitors as potential cancer treatments. One of these inhibitors currently used for the treatment of colorectal and head and neck cancers is Cetuximab , a monoclonal antibody, which inhibits EGF receptors.
Bio-Rad offers a variety of antibodies for analyzing kinases by ELISA, Flow Cytometry, Immunofluorescence, Immunohistochemistry and Western Blotting. For your convenience, we have grouped our research reagents into the main seven kinase families:
De Lartigue J (2011). Phosphorylation: The Master Switch of the Cell. http://www.onclive.com/publications/Oncology-live/2011/november-2011/Phosphorylation-The-Master-Switch-of-the-Cell, accessed June 29, 2015.
Martin et al. (2008). Kinomer v. 1.0: a database of systematically classified eukaryotic protein kinases Nucleic Acids Research, doi: 10.1093/nar/gkn834.
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