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Mouse Anti-RPA2 Recombinant Antibody (CBT2782) (V2LY-0625-LY1928)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBT2782
Antibody Isotype
IgG1, κ
Application
WB, IHC, FC

Basic Information

Immunogen
Purified recombinant fragment of human RFA2 expressed in E. Coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:500-1:2,000
IHC-P1:200-1:1,000
FC1:200-1:400

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
Sodium azide
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Replication Protein A2
Entrez Gene ID
6118
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.
Biological Process
Base-excision repairManual Assertion Based On ExperimentIDA:UniProtKB
DNA replicationManual Assertion Based On ExperimentIDA:UniProtKB
Double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:UniProtKB
Mismatch repairManual Assertion Based On ExperimentIMP:UniProtKB
Mitotic G1 DNA damage checkpoint signalingManual Assertion Based On ExperimentIMP:UniProtKB
Nucleotide-excision repairManual Assertion Based On ExperimentIMP:UniProtKB
Protein localization to chromosomeManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of DNA damage checkpointManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:UniProtKB
Telomere maintenanceManual Assertion Based On ExperimentIMP:UniProtKB
Cellular Location
Nucleus
Nucleus, PML body
Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner.
PTM
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 (PubMed:24332808).
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 (PubMed:26474068).
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For research use only. Not intended for any clinical use.

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