|Calculated MW||68138 Da|
|Other Names||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|
|Target/Specificity||A synthetic peptide corresponding to residues in human RPA 70 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RPA-70 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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 (PubMed:27723720, PubMed:27723717). 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). 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).|
|Cellular Location||Nucleus. Nucleus, PML body. Note=Enriched in PML bodies in cells displaying alternative lengthening of their telomeres.|
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Provided below are standard protocols that you may find useful for product applications.
Replication protein A (RPA) is a single-stranded DNA-binding (ssDNA) protein involved in multiple processes of eukaryotic DNA metabolism, including DNA replication, repair, and recombination. It is found to be essential for replication of the papovavirus SV40 (1). RPA is a complex of three polypeptides of 70, 34, and 13 kDa (2). The DNA-binding activity may reside exclusively on the 70-kDa subunit RPA 70. The 70-kDa subunit of RPA (RPA 70) is composed of three functional domains consisting of an N-terminal domain that is not required for ssDNA binding or SV40 replication, a central DNA-binding domain, and a C-terminal domain that is essential for subunit interactions (3).
1. Park J., et al. Mol. Cell. Biol. 25:8202-8214, 2005 2. Keshav K.F., et al. Mol. Cell. Biol. 15:3119-3128, 1995 3. Gomes XV, et al. Biochemistry 35(32):10558-68, 1996
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