Anti-Phospho-RPA p32 (S33) antibody

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Product name Anti-Phospho-RPA p32 (S33) antibody
Short Description Rabbit polyclonal against Phospho-RPA p32 (S33)
Description Rabbit polyclonal to Phospho-RPA p32 (S33).
Applications ELISA, WB
Dilution range WB 1:500-1:2000
ELISA 1:10000
Specificity Phospho-RPA p32 (S33) polyclonal antibody detects endogenous levels of RPA p32 protein only when phosphorylated at S33.
Protein Name 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
Immunogen Synthesized peptide derived from human RPA p32 around the phosphorylation site of S33.
Immunogen Region 10-90 aa
Storage Instruction Store at-20°C, and avoid repeat freeze-thaw cycles.
Host Rabbit
Clonality Polyclonal
Reactivity Human, Mouse, Rat
Conjugation Unconjugated
Concentration 1 mg/ml
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 6118
Gene Symbol RPA2
Molecular Weight 32 kDa
Database Links HGNC:10290
Alternative Names Anti-Replication Protein A 32 Kda Subunit antibody
Anti-Rp-A P32 antibody
Anti-Replication Factor A Protein 2 antibody
Anti-Rf-A Protein 2 antibody
Anti-Replication Protein A 34 Kda Subunit antibody
Anti-Rp-A P34 antibody
Anti-RPA2 REPA2 RPA32 RPA34 antibody
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.
Post-translational Modifications Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.; DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination.
Cellular Localization Nucleus
Pml Body
Redistributes To Discrete Nuclear Foci Upon Dna Damage In An Atr-Dependent Manner
Swiss-Prot Key RFA2_HUMAN
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