CDK9 (Cyclin-Dependent Kinase 9) is a serine/threonine kinase integral to transcriptional regulation as a component of the positive transcription elongation factor b (P-TEFb) complex. It phosphorylates the C-terminal domain of RNA polymerase II, enabling transcriptional elongation and regulating the expression of genes critical for cell growth, differentiation, and stress responses. CDK9’s role in promoting the transcription of pro-survival and oncogenic proteins, such as MYC and MCL-1. has linked its dysregulation to cancers, viral replication (e.g., HIV), and inflammatory diseases.
CDK9 antibodies are essential tools for studying its expression, localization, and interactions in cellular processes. These antibodies are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to assess CDK9 protein levels, activation states (e.g., phosphorylation at Thr-186), and association with cyclin partners (e.g., Cyclin T1/T2). Researchers also employ CDK9 antibodies to explore its therapeutic targeting, particularly in cancer, where CDK9 inhibitors are being investigated to suppress oncogene transcription.
Specificity is a key consideration, as CDK9 shares homology with other CDKs. High-quality antibodies distinguish CDK9 from related kinases (e.g., CDK7) and detect post-translational modifications. Their applications extend to drug development, biomarker studies, and mechanistic research in diseases like leukemia, solid tumors, and viral infections. Recent studies also highlight CDK9’s involvement in epigenetic regulation, expanding the utility of these antibodies in interdisciplinary research.