Phospho-CDC37 (Ser13)抗体;Phospho-CDC37 (Ser13) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-Cdc37 (Ser13) in mouse liver lysates using Phospho-CDC37 (Ser13) antibody.    

  
  

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     Western blot analysis of Cdc37 (Phospho-Ser13) in Hela, rat Brain, Ramos lysates using Cdc37 (Phospho-Ser13) antibody.    

  
  

Phospho-CDC37 (Ser13) antibodies are essential tools for studying the post-translational modification of CDC37. a co-chaperone protein critical for regulating the heat shock protein 90 (HSP90) chaperone machinery. CDC37 facilitates client protein recruitment, particularly kinases, to HSP90. ensuring their proper folding, stability, and activation. Phosphorylation at Ser13 is a key regulatory mechanism modulating CDC37 function. This modification enhances its interaction with HSP90 and promotes the maturation of client kinases, including oncogenic kinases like AKT, BRAF, and CDK4.

The phosphorylation event at Ser13 is mediated by kinases such as CDK5 or CK2. depending on cellular context, and is often linked to cellular stress responses, proliferation, or tumorigenesis. Dysregulation of CDC37 phosphorylation has been implicated in cancer progression, neurodegenerative diseases, and inflammatory conditions.

Phospho-CDC37 (Ser13) antibodies specifically detect this phosphorylated form, enabling researchers to study CDC37 activation status, its association with HSP90-client complexes, and downstream signaling pathways. These antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore disease mechanisms or evaluate therapeutic interventions targeting the HSP90-CDC37 axis. Their specificity makes them valuable for investigating how post-translational modifications fine-tune chaperone-mediated protein homeostasis in health and disease.