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RPA, best known for its role in DNA replication and repair, recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation.
Single point mutations in the RPA32 subunit of RPA that abolish interaction with RFWD3 also inhibit interstrand crossling repair, demonstrating that RPA-mediated RFWD3 recruitment to stalled replication forks is important for ICL repair.
E3 ligase RFWD3 (show RFWD3 Proteins) functions in timely removal and degradation of RPA (show RPA1 Proteins) and RAD51 (show RAD51 Proteins) to allow homologous recombination progression to subsequent steps following mitomycin C damage.
knockdown of RPA2 promoted formation of the menin-p65 (show GORASP1 Proteins) complex and repressed the expression of NF-kappaB (show NFKB1 Proteins)-mediated genes. RPA2 expression was induced via an E2F1 (show E2F1 Proteins)-dependent mechanism in MCF7 and MDA-MB-231 cells treated with NF-kappaB (show NFKB1 Proteins) activators, TNF-alpha (show TNF Proteins) or lipopolysaccharide (LPS (show IRF6 Proteins)).
The authors show that Vpr can form a trimolecular complex with UNG2 (show CCNO Proteins) and RPA32 and the positive effect of UNG2 (show CCNO Proteins) and RPA32 on the reverse transcription process leading to optimal virus replication and dissemination between the primary target cells of HIV-1.
RPA32 phosphorylation regulates replication arrest, recombination, late origin firing, and mitotic catastrophe
Expression of mutant RPA2 or loss of PALB2 expression led to significant DNA damage after replication stress, a defect accentuated by poly-ADP (adenosine diphosphate) ribose polymerase inhibitors.
Conserved motifs are required for RPA32 binding the the N-terminus of SMARCAL1 (show SMARCAL1 Proteins).
study reports the characterization of the RPA32C-SMARCAL1 (show SMARCAL1 Proteins) interface at the molecular level; implications of results are discussed with respect to the recruitment of SMARCAL1 (show SMARCAL1 Proteins) and other DNA damage response and repair proteins to stalled replication forks
study concludes RPA2 expression is translationally regulated via internal ribosome entry site and by eIF3a (show EIF6 Proteins) and that this regulation is partly accountable for cellular response to DNA damage and survival.
Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage (By similarity). Required for simian virus 40 DNA replication in vitro. It participates in a very early step in initiation.
RF-A protein 2
, RP-A p32
, RP-A p34
, replication factor A protein 2
, replication protein A 32 kDa subunit
, replication protein A 34 kDa subunit
, replication protein A, subunit 2
, replication protein A2
, p32-subunit of replication protein A
, RPA p32
, replication protein A2, 32kDa
, putative replication protein A middle subunit
, 30-kDa protein