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RFA2 Antibody
Purified Mouse Monoclonal Antibody (Mab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P15927 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | monoclonal |
| Isotype | IgG1,k |
| Clone/Animal Names | 1591CT183.68.6 |
| Calculated MW | 29247 Da |
| Gene ID | 6118 |
|---|---|
| Other Names | Replication protein A 32 kDa subunit, RP-A p32, Replication factor A protein 2, RF-A protein 2, Replication protein A 34 kDa subunit, RP-A p34, RPA2, REPA2, RPA32, RPA34 |
| Target/Specificity | This RFA2 antibody is generated from a mouse immunized with a recombinant protein of human RFA2. |
| Dilution | WB~~1:4000 IHC-P~~1:25 |
| Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | RFA2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RPA2 |
|---|---|
| Synonyms | REPA2, RPA32, RPA34 |
| 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. Also plays 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. RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542). |
| Cellular Location | Nucleus. Nucleus, PML body. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. 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.
References
Erdile L.F.,et al.J. Biol. Chem. 265:3177-3182(1990).
Ebert L.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
Gregory S.G.,et al.Nature 441:315-321(2006).
Din S.,et al.Genes Dev. 4:968-977(1990).
Dutta A.,et al.EMBO J. 11:2189-2199(1992).
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