Phospho-Cyclin E (Thr62) Antibody detects endogenous levels of cyclin E only when phosphorylated at threonine 62 (cyclin E1 isoform 2) or threonine 77 (cyclin E1 isoform 1).
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr62 of human cyclin E. Antibodies are purified by protein protein A and peptide affinity chromatography.
Background
Cyclin E1 and cyclin E2 can associate with and activate CDK2 (1). Upon DNA damage, upregulation/activation of the CDK inhibitors p21 Waf1/Cip1 and p27 Kip1 prevent cyclin E/CDK2 activation, resulting in G1/S arrest. When conditions are favorable for cell cycle progression, cyclin D/CDK4/6 phosphorylates Rb and is thought to reduce the activity of p21 Waf1/Cip1 and p27 Kip1, allowing subsequent activation of cyclin E/CDK2 (1,2). Cyclin E/CDK2 further phosphorylates Rb to allow progression into S-phase, where cyclin E/CDK2 is thought to phosphorylate and activate multiple proteins involved in DNA synthesis (2,3). Turnover of cyclin E is largely controlled by phosphorylation that results in SCFFbw7-mediated ubiquitination and proteasome-dependent degradation (4,5). Cyclin E1 is phosphorylated at multiple sites in vivo including Thr62, Ser88, Ser72, Thr380 and Ser384, and is controlled by at least two kinases, CDK2 and GSK-3 (6,7).
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