HJURP抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P10600(HJURP Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P10600(HJURP Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

HJURP (Holliday Junction Recognition Protein) is a centromere-associated protein critical for recruiting and stabilizing CENP-A, a histone H3 variant essential for centromere specification and kinetochore assembly during cell division. As a chaperone, HJURP ensures the precise deposition of CENP-A into centromeric chromatin, maintaining genomic stability by facilitating proper chromosome segregation. Its role in centromere maintenance links HJURP to cell cycle regulation, particularly during the G1/S phase when CENP-A replenishment occurs.

Antibodies targeting HJURP are vital tools for studying its function, localization, and expression dynamics in both normal and pathological contexts. Researchers use these antibodies in techniques like immunofluorescence, western blotting, and chromatin immunoprecipitation (ChIP) to investigate HJURP-CENP-A interactions and their impact on mitotic fidelity.

HJURP dysregulation is implicated in cancers, including hepatocellular carcinoma, breast cancer, and lung cancer, where its overexpression correlates with poor prognosis, genomic instability, and therapeutic resistance. Anti-HJURP antibodies thus also serve as potential biomarkers for cancer diagnosis or targets for drug development. Recent studies explore HJURP's interplay with other centromere components and its post-translational modifications, deepening insights into centromere biology and diseases linked to chromosomal missegregation.