MW 294.14 Da, Purity >97%. Selectively inhibits Na+/H+ exchangers in cellular membranes, resulting in the retention of H+ ions and in the decrease of intracellular pH. Also blocks TRPA1 channels (IC50 = 80 µM).
DNA repair protein RAD52, DNA repair protein RAD52 homolog, RAD52 homolog, RAD52 homolog (S. cerevisiae), RAD52_HUMAN, Recombination protein RAD52, Rhabdomyosarcoma antigen MU RMS 40.23
MW 294.14 Da, Purity >97%. Selectively inhibits Na+/H+ exchangers in cellular membranes, resulting in the retention of H+ ions and in the decrease of intracellular pH. Also blocks TRPA1 channels (IC50 = 80 µM).
Soluble in DMSO to 10 mM.
Selectively inhibits Na+/H+ exchangers in cellular membranes, resulting in the retention of H+ ions and in the decrease of intracellular pH. Also blocks TRPA1 channels (IC50 = 80 µM).
RAD52 also known by alternate names such as DNA repair protein RAD52 homolog functions as an important player in DNA repair mechanisms. It aids in the homologous recombination and repair of DNA double-strand breaks. RAD52 has a molecular mass of approximately 49 kDa and is mainly expressed in the nucleus. Its ability to bind to DNA and facilitate strand annealing are important for its mechanical function. RAD52 expression varies across tissues but it is prominently observed in rapidly dividing cells and tissues with high rates of DNA repair activity.
DNA repair protein RAD52 homolog engages significantly in maintaining genome stability. RAD52 forms complexes with other DNA repair proteins such as RAD51 and RPA to perform its role efficiently. The protein supports the loading of RAD51 onto single-stranded DNA a critical step in homologous recombination. By stabilizing RAD51 nucleoprotein filaments RAD52 promotes efficient repair and recombination processes necessary for cellular survival after DNA damage.
The activities of RAD52 link to the homologous recombination and DNA damage response pathways. RAD52 operates alongside proteins like RAD51 and BRCA2 to mediate the repair of DNA double-strand breaks through homologous recombination. This relationship is important for maintaining genomic integrity especially during the S and G2 phases of the cell cycle. The synergy between RAD52 and other double-strand break repair proteins ensures effective resolution of DNA damage.
The malfunction or dysregulation of RAD52 connects to conditions like cancer and Fanconi anemia. Deficiencies or mutations in RAD52 can compromise DNA repair and lead to genomic instability a hallmark of cancer. Additionally in Fanconi anemia the interplay between RAD52 and the FA complex is impaired influencing the DNA repair capacity. The disrupted interaction with other repair proteins including those in the BRCA family further suggests RAD52's important role in disease pathogenesis.
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2D chemical structure image of ab145569, Dimethylamiloride hydrochloride (5-(N,N-Dimethyl)amiloride hydrochloride), Na+/H+ exchange blocker
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