Anti-RPA14 Antibody (56215)

N-terminally 6x-His tagged fusion protein corresponding to full-length human RPA14 expressed in E. coli.

PBS, pH 7.4

Liquid

Purified by Protein G affinity chromatography

This antibody is stable for at least one (1) year at -70°C. Avoid multiple freeze- thaw cycles.

Research Use Only

Next Day 2-8°C

This antibody recognizes human and mouse RPA14. 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.

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. 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. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). 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). {PubMed:19010961, PubMed:19116208, PubMed:19996105, PubMed:7697716, PubMed:9430682, PubMed:9765279, PubMed:24332808}.

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