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     Western blot analysis of Cdk1/2 (Phospho-Thr14) in HepG2, U2OS, U251 lysates using Phospho-CDK1/2 (Thr14) antibody.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human lung cancer using Cdk1/2 (Phospho-Thr14) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

Phospho-CDK1/2 (Thr14) antibodies are essential tools for studying the regulation of cyclin-dependent kinases 1 and 2 (CDK1 and CDK2), which are critical regulators of cell cycle progression. CDK1. primarily involved in the G2/M transition, and CDK2. which governs the G1/S and S phase transitions, are tightly controlled by post-translational modifications, including inhibitory phosphorylation at specific residues. Phosphorylation at Thr14. located in the ATP-binding pocket of these kinases, is a key regulatory mechanism that suppresses their enzymatic activity. This modification is mediated by kinases such as WEE1 and MYT1 in response to DNA damage or incomplete replication, ensuring cell cycle arrest to allow repair or prevent genomic instability.

Antibodies targeting phosphorylated Thr14 in CDK1/2 enable researchers to detect and quantify this inhibitory modification in various experimental settings, including Western blotting, immunofluorescence, and immunoprecipitation. These antibodies are widely used to investigate cell cycle checkpoints, DNA damage response pathways, and the effects of therapeutic agents targeting CDK activity. Specificity validation, including knockout controls and peptide competition assays, is crucial to confirm their reliability. Such studies have highlighted the role of Thr14 phosphorylation in diseases like cancer, where dysregulated CDK activity contributes to uncontrolled proliferation. By monitoring Thr14 phosphorylation status, researchers gain insights into cellular stress responses and the efficacy of CDK-targeted therapies.