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Antibodies for the analysis of kinases
Western blot analysis of whole cell lysates probed with AKT1 antibody followed by detection with HRP conjugated Goat Anti-Mouse IgG (1/10,000, STAR207P) and visualized on the ChemiDoc MP with 19 second exposure. Arrow points to AKT1 (molecular weight 60 kDa).
During a phosphorylation event, a phosphate group is added by a kinase to a serine, threonine or tyrosine residue of a target protein. This process can be reversed by another group of enzymes called phosphatases.
Both kinases and phosphatases are specific with regards to whether they phosphorylate or dephosphorylate tyrosine or serine/threonine residues. Philip Cohen stated that “the reversible phosphorylation of proteins regulates nearly every aspect of cell life” (Cohen 2002). 518 kinases are encoded in the human genome (Manning et al. 2002; Ferguson and Gray 2018), which play a pivotal role in regulating cellular processes (Walsh et al. 2005; Ubersax and Ferrell 2007).
Protein kinases have developed a series of mechanisms to ensure specificity, for example structurally characteristic active sites and binding partners that ensure the kinase only phosphorylates its specific substrates (Ubersax and Ferrell 2007).
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, 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 seven main kinase families: