Anti-RPA32 Antibody

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {PubMed:15205463, PubMed:17765923, PubMed:17959650, PubMed:19116208, PubMed:20154705, PubMed:21504906, PubMed:2406247, PubMed:24332808, PubMed:7697716, PubMed:7700386, PubMed:8702565, PubMed:9430682, PubMed:9765279}.

This antibody recognizes human and mouse RPA32. RPA (Replication Protein A) is a single-stranded DNA binding protein. Human RPA is a heterotrimeric protein containing subunits of 70, 32, and 14 kD. This protein complex is highly conserved in eukaryotes and is essential in DNA replication, homologous recombination, and nucleotide excision repair. RPA32 is phosphorylated during the S-phase of the cell cycle, in response to DNA damage, and during apoptosis of Jurkat T-lymphocytes.