ELOC抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P10229(ELOC Antibody) at dilution 1/55. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human ovarian cancer tissue using P10229(ELOC Antibody) at dilution 1/55. (Original magnification: ×200)    

  
  

The ELOC antibody targets the Elongin C (ELOC) protein, a critical component of the Elongin complex, which plays multifaceted roles in transcriptional regulation and protein ubiquitination. ELOC, also known as TCEB1. forms a heterotrimeric complex with Elongin A (ELOA) and Elongin B (ELOB) to enhance RNA polymerase II transcriptional elongation by suppressing transient pausing. Additionally, ELOC interacts with the von Hippel-Lindau (VHL) tumor suppressor protein as part of the VHL-Elongin B-Elongin C (VBC) complex, which functions as a substrate-recognition module in the Cullin 2 (CUL2)-based E3 ubiquitin ligase. This ligase targets hypoxia-inducible factor (HIF) for proteasomal degradation under normoxic conditions, a key regulatory mechanism in oxygen sensing and tumor suppression.

ELOC antibodies are essential tools for studying its dual roles in transcription and ubiquitination. They are used to investigate ELOC expression, complex formation, and dysregulation in diseases like renal cell carcinoma (linked to VHL mutations) or other cancers where HIF signaling is aberrant. Researchers employ these antibodies in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry to explore ELOC’s involvement in cellular responses to hypoxia, DNA repair, and tumorigenesis. The development of specific ELOC antibodies has advanced understanding of its structural interactions within the Elongin and VBC complexes, as well as its broader implications in gene expression and protein stability pathways.