p23抗体;p23 Antibody—艾普蒂 新品

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     Western blot analysis of p23 expression in (1) HeLa cell lysate; (2) NIH/3T3 cell lysate; (3) PC12 cell lysate.    

  
  

The p23 antibody targets the p23 protein, a co-chaperone of the heat shock protein 90 (HSP90) complex. First identified in the 1990s, p23 plays a critical role in stabilizing HSP90-client protein interactions, facilitating the conformational maturation of diverse client proteins, including steroid hormone receptors, kinases, and transcription factors. Its ATPase activity and ability to bind HSP90 during the late stages of the chaperone cycle make it essential for maintaining proteostasis and regulating cellular stress responses.

p23 is overexpressed in various cancers, where it supports tumorigenesis by stabilizing oncogenic clients like HER2. AKT, and mutant p53. This association has driven interest in p23 as a potential therapeutic target and biomarker. Researchers use p23 antibodies in techniques such as Western blotting, immunohistochemistry, and co-immunoprecipitation to study its expression, localization, and interactions in normal and diseased tissues.

Recent studies also explore p23’s role in non-cancer pathologies, including neurodegenerative diseases and viral infections, where HSP90-client pathways are dysregulated. Despite its importance, p23’s regulatory mechanisms and tissue-specific functions remain incompletely understood, prompting ongoing research to clarify its broader biological and clinical implications.