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RPA2 / RFA2 / RPA34 Antibody

Rabbit Polyclonal Antibody

     
  • WB - RPA2 / RFA2 / RPA34 Antibody ALS16176
    Western blot of Replication protein A 32 kDa subunit antibody at 2 ug/ml.
    detail
  • IHC - RPA2 / RFA2 / RPA34 Antibody ALS16176
    Anti-RPA2 / RFA2 / RPA34 antibody IHC staining of human prostate.
    detail
  • SPECIFICATION
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  • BACKGROUND
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P, E
Primary Accession P15927
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 29kDa
Dilution IHC-P (10 µg/ml)
Additional Information
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 Human RPA2 / RFA2 / RPA34
Reconstitution & Storage Aliquot and store at -20°C or -80°C. Avoid freeze-thaw cycles.
PrecautionsRPA2 / RFA2 / RPA34 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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.
Cellular Location Nucleus. Nucleus, PML body. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner
Citations (0)
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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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Discontinued
Cat# ALS16176
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