**Background of PJA1 Antibody**
PJA1 (Praja Ring Finger Ubiquitin Ligase 1) is an E3 ubiquitin ligase belonging to the PHD finger protein family, primarily involved in the ubiquitin-proteasome system (UPS). It facilitates substrate-specific protein ubiquitination, marking target proteins for degradation or functional modulation. PJA1 contains a conserved RING finger domain critical for its ligase activity and a PHD zinc finger domain implicated in protein interactions.
Research highlights PJA1's role in regulating key cellular processes, including cell cycle progression, signal transduction, and gene expression. It interacts with substrates such as kinases (e.g., AKT) and transcription factors, influencing pathways like Wnt/β-catenin and Notch, which are pivotal in development and disease. Dysregulation of PJA1 has been linked to cancer, neurodegenerative disorders, and cardiovascular diseases, with studies showing altered expression in tumors, where it may promote proliferation or metastasis.
PJA1 antibodies are essential tools for detecting PJA1 expression, localization, and interaction partners in experimental models. They enable investigations into its physiological and pathological roles via techniques like Western blotting, immunohistochemistry, and co-immunoprecipitation. Understanding PJA1's mechanisms may unveil therapeutic targets for diseases linked to UPS dysfunction.