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RPA32 Antibody

Rabbit Monoclonal Antibody

  • WB - RPA32 Antibody AJ1695a
    A. Western blot analysis on (A) HeLa, (B) HUVEC, (C) NIH/3T3 and (D) C6 cell lysates using anti-RPA32 RabMAb (Cat. #AJ1695a), dilution 1:10,000.
  • IHC - RPA32 Antibody AJ1695a
    B. Immunohistochemical analysis of paraffin-embedded human breast carcinoma using anti-RPA32 RabMAb (Cat. #AJ1695a).
Product Information
  • 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
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P15927
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Monoclonal
Clone Names EPR2877Y
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 A synthetic peptide corresponding to residues on the C terminus of human RPA32 was used as an immunogen.
Dilution WB~~1:1000~10000
Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
StorageMaintain 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.
PrecautionsRPA32 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. Plays also 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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Replication protein A (RPA) is a heterotrimeric single-stranded DNA-binding protein that plays essential roles in nucleic acid metabolism, including DNA replication, nucleotide excision repair, and homologous recombination. It is a complex of three polypeptides of molecular mass 70, 32, and 14 kDa (RPA70, RPA32, and RPA14). RPA is a phosphorylation target for DNA-dependent protein kinase (DNA-PK) and likely the ataxia telangiectasia-mutated gene (ATM) protein kinase. The middle subunit, RPA32, is phosphorylated in a cell cycle-dependent manner which begins in parallel to the degradation of DNA to high molecular weight fragments, and slowly continues until late apoptosis. Hyperphosphorylation of RPA32 requires the activities of DNA-dependent protein kinase and of a cyclin-dependent protein kinase (1-3). RPA32 has been reported to be a useful prognostic indicator in colon cancer patients and an attractive therapeutic target for regulation by tumor suppressors or other proteins involved in the control of cell proliferation (4).


1. Treuner K, et al. Nucleic Acids Research 27(6):1499-1504, 1999
2. Iftode C, et al. Biochem. Mol. Biol. 34(3):141-80, 1999
3. Treuner K, et al. J Biol Chem. 274(22):15556-15561, 1999
4. Givalos N, et al. Modern Pathology 20:159-166, 2007

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Cat# AJ1695a
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