|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||29247 Da|
|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.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|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||RPA32 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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|
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Provided below are standard protocols that you may find useful for product applications.
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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