|Application ||WB, IHC, FC, ICC, E|
|Description||"This gene Plays an essential role in several cellular processes in DNA metabolism including replication, recombinationand DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementaryDNA from reannealing"|
|Immunogen||Purified recombinant fragment of human RPA1 expressed in E. Coli. |
|Formulation||Purified antibody in PBS with 0.05% sodium azide|
|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|
WB~~1/500 - 1/2000
IHC~~1/200 - 1/1000
IF~~1/200 - 1/1000
FC~~1/200 - 1/400
|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||RPA1 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). 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).|
|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.
Mol Cell. 2009 Oct 23;36(2):193-206. J Biol Chem. 2009 Dec 11;284(50):34682-91.
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