USP53抗体

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P09847(USP53 Antibody) at dilution 1/130. (Original magnification: ×200)    

  
  

The USP53 antibody targets ubiquitin-specific protease 53 (USP53), a deubiquitinating enzyme belonging to the ubiquitin-specific protease (USP) family. USP53 regulates protein stability and function by cleaving ubiquitin chains from substrate proteins, thereby modulating cellular processes like protein degradation, signal transduction, and stress responses. Primarily expressed in the liver, kidney, and gastrointestinal tract, USP53 has been linked to bile acid homeostasis and cholestatic liver diseases. Mutations in the USP53 gene are associated with progressive familial intrahepatic cholestasis (PFIC), highlighting its role in maintaining hepatobiliary function.

USP53 antibodies are essential tools for studying the enzyme's expression, localization, and interaction partners. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Researchers use these antibodies to explore USP53's involvement in diseases, such as liver disorders, cancer (e.g., colorectal and hepatocellular carcinoma), and metabolic syndromes, where dysregulated deubiquitination may drive pathogenesis. Commercial USP53 antibodies are typically validated for specificity using knockout cell lines or tissues to minimize cross-reactivity with other USPs. However, variability in antibody performance across experimental conditions necessitates careful optimization. Ongoing studies aim to clarify USP53's mechanistic roles and therapeutic potential, positioning it as a biomarker or drug target in precision medicine.