Phospho-CDK1/2/3-T14 Rabbit mAb - P06493/P24941/Q00526

Core Product Specifications and Parameters

Biological Background: CDK1/2/3 Function and Localization

• Cyclin-dependent kinase 1 (CDK1), also known as cell division control protein 2 homolog (CDC2) or p34 protein kinase, is a serine/threonine-protein kinase essential for eukaryotic cell cycle progression. Related references: PMID:16407259 PMID:16933150 PMID:17459720
• CDK1, in complex with cyclins, promotes the G2-M transition and regulates mitotic onset by phosphorylating numerous substrates, including nuclear lamins, histones, and cytoskeletal proteins. Related references: PMID:18480403 PMID:20360007 PMID:2188730
• CDK1 activity is tightly controlled by phosphorylation: WEE1 and PKMYT1 kinases phosphorylate Tyr15 and Thr14 to inhibit CDK1, while CDC25 phosphatases remove these phosphates to trigger mitotic entry. Related references: PMID:18480403 PMID:20360007
• CDK1 localizes to the nucleus, cytoplasm, centrosome, and mitotic spindle, reflecting its coordinated roles in nuclear envelope breakdown, centrosome separation, and spindle assembly.
• Beyond its classical cell cycle functions, CDK1 phosphorylation of various substrates also influences apoptosis (e.g., Bcl-xL, CASP8), transcriptional regulation (e.g., FOXO1, EZH2), and circadian rhythms. Related references: PMID:19917720 PMID:20937773 PMID:18356527 PMID:20935635 PMID:27238018
• CDK1 is found in breast cancer tissues and also acts as a receptor for hepatitis C virus (HCV) entry, highlighting its relevance in disease contexts.

Experimental Guidance and Technical Tips

• The immunogen is a synthetic phosphorylated peptide around T14 of human CDK1 (P06493), which is conserved in CDK1, CDK2, and CDK3; therefore, the antibody may detect all three kinases when phosphorylated at this inhibitory site.
• Thr14 phosphorylation is an inhibitory modification; consider using this antibody to monitor CDK1/2/3 inactivation during cell cycle checkpoints and DNA damage responses.
• For WB, the expected molecular weight is approximately 34 kDa; it is advisable to include appropriate phosphatase inhibitors in lysis buffers to preserve phosphorylation.
• For ELISA, the phospho-specific nature of the antibody makes it suitable for quantifying phosphorylation levels; validate in relevant sample systems, such as synchronized cell extracts.
• Cross-reactivity with mouse and rat is reported, enabling studies in common model organisms.

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