Anti-RPA32 / Replication Protein A2, clone RPA2/3140R

0.2 mg/ml with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Recognizes a protein of 34kDa, identified as a subunit of Replication Protein A (RPA) (also known as human single-stranded DNA binding protein, or HSSB). RPA from human cells is a stable heterotrimer of 70kDa, 32-34kDa, and 11-14kDa subunits (RPA70, RPA32, and RPA14 respectively). It is involved in DNA replication, repair, and recombination. RPA is required for the SV40 large tumor antigen-catalyzed unwinding of SV40 DNA and stimulates DNA polymerase (pol) alpha and delta. RPA34 is phosphorylated at the G1/S boundary of the cell cycle or upon exposure of cells to DNA damage-inducing agents including ionizing and UV radiation. Protein function: 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. [The UniProt Consortium]