Anti-RPA70/RPA1 Antibody Picoband® Fluoro647 Conjugated

Replication protein A 70 kDa DNA-binding subunit is a protein that in humans is encoded by the RPA1 gene. This gene is mapped to chromosome 17p13.3. Replication protein A (RPA) is a heterotrimeric single-strand DNA (ssDNA) -binding protein essential for DNA replication, repair, and recombination. It is composed of 70-kD (RPA1), 32-kD (RPA2), and 14-kD (RPA3) subunits. The RPA1 subunit is responsible for high-affinity ssDNA binding. The RPA complex was originally isolated as a factor essential for in vitro replication of the papovavirus SV40. It had been found that recombinant human RPA1, purified from bacteria, exhibited ssDNA-binding activity comparable to that of the complete RPA complex. RPA1 could substitute for the complete complex in stimulating the activity of DNA polymerase alpha-primase, but it could not substitute for the complete complex in SV40 DNA replication in vitro, suggesting an important functional role for the other subunits.

Replication protein A 70 kDa DNA-binding subunit; RP-A p70; Replication factor A protein 1; RF-A protein 1; Single-stranded DNA-binding protein; Replication protein A 70 kDa DNA-binding subunit, N-terminally processed; RPA1; REPA1, RPA70

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 (PubMed:9430682) . 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 (PubMed:24332808) . It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923) . 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 (PubMed:7697716) . Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279) . Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. 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:17959650) . As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2- containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105) . .

1. Erdile, L. F., Heyer, W.-D., Kolodner, R., Kelly, T. J. Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication. J. Biol. Chem. 266: 12090-12098, 1991. Note: Erratum: J. Biol. Chem. 268: 2268 only, 1993. 2. Haring, S. J., Mason, A. C., Binz, S. K., Wold, M. S. Cellular functions of human RPA1: multiple roles of domains in replication, repair, and checkpoints. J. Biol. Chem. 283: 19095-19111, 2008.