ELOB (Elongin B) is a critical subunit of the Elongin complex, which plays dual roles in transcriptional regulation and protein ubiquitination. The Elongin complex consists of Elongin A (a transcription elongation factor), Elongin B, and Elongin C. Structurally, ELOB and ELOC form a stable heterodimer that interacts with Elongin A to enhance RNA polymerase II processivity during transcription. Additionally, ELOB/ELOC serves as a core component of the von Hippel-Lindau (VHL) tumor suppressor complex, which functions as an E3 ubiquitin ligase targeting hypoxia-inducible factor (HIF-1α) for proteasomal degradation.
ELOB antibodies are widely used to study these molecular mechanisms, particularly in cancer research. Dysregulation of ELOB-containing complexes is linked to tumorigenesis, as seen in VHL syndrome where mutations disrupt HIF-1α degradation, promoting angiogenesis and tumor growth. Researchers employ ELOB antibodies in techniques like Western blotting, immunoprecipitation, and immunohistochemistry to analyze protein expression, complex formation, and subcellular localization. These tools help elucidate ELOB's role in cellular responses to hypoxia, DNA repair, and its interplay with oncogenic pathways.
The specificity and reliability of ELOB antibodies make them essential for investigating transcriptional elongation, ubiquitination pathways, and therapeutic targets in diseases like renal cell carcinoma. Their application continues to advance understanding of ELOB's regulatory functions in both normal physiology and pathology.