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Phospho-RPA32/RPA2 (T21) (10A4) Monoclonal Antibody

Product Specifications

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.

Synonyms

Replication protein A 32 kDa subunit, Replication factor A protein 2, Replication protein A 34 kDa subunit, RP-A p32, RF-A protein 2, RP-A p34, RPA2, REPA2, RPA32, RPA34

Swiss Prot

P15927

Modification Site

T21

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat

Target

Phospho-RPA32/RPA2 (T21)

Clonality

Monoclonal

Isotype

IgG

Clone

10A4

Conjugation

Unconjugated

Source

Synthetic phospho-peptide surrounding Thr21 of human RPA32/RPA2

Applications

WB

Purification

Purified by Protein A.

Concentration

1µg/µl

Dilution

WB (1:300-5000)

Buffer

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Phosphorylation

Storage Conditions

Store at -20°C for 12 months.

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