Rabbit Polyclonal CyclinH(Phospho-Thr315) Antibody

Cyclin H, a regulatory subunit of the cyclin-dependent kinase (CDK)-activating kinase (CAK) complex, plays a critical role in cell cycle progression and transcriptional regulation. The CAK complex, composed of Cyclin H, CDK7. and MAT1. phosphorylates CDKs (e.g., CDK1. CDK2. CDK4/6) to activate their kinase activity, driving cell cycle transitions. Additionally, CDK7 functions as a component of the general transcription factor TFIIH, facilitating RNA polymerase II-mediated transcription. Phosphorylation of Cyclin H at Thr315 is a post-translational modification implicated in modulating the activity or stability of the CAK complex. This phosphorylation event may influence interactions within the complex or its substrate recognition, potentially impacting both cell cycle control and transcriptional processes. Antibodies specific for Cyclin H phosphorylated at Thr315 (Phospho-Thr315) are essential tools for studying the regulatory mechanisms of CAK in physiological and pathological contexts, such as cancer, where dysregulated CDK activity is common. These antibodies enable detection of the phosphorylated form via techniques like Western blotting, immunofluorescence, or immunoprecipitation, helping researchers assess Cyclin H activation status in response to cellular signals or therapeutic interventions. Validation of such antibodies typically includes testing in knockout models or phosphorylation-deficient mutants to ensure specificity.