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Human Polyclonal RPA1 Primary Antibody for IHC (p), IHC - ABIN151627
Thangavel, Mendoza-Maldonado, Tissino, Sidorova, Yin, Wang, Monnat, Falaschi, Vindigni: Human RECQ1 and RECQ4 helicases play distinct roles in DNA replication initiation. in Molecular and cellular biology 2010
Show all 6 Pubmed References
Yeast (Saccharomyces cerevisiae) Polyclonal RPA1 Primary Antibody for ChIP, IP - ABIN190714
Chen, Lisby, Symington: RPA coordinates DNA end resection and prevents formation of DNA hairpins. in Molecular cell 2013
Show all 5 Pubmed References
Human Monoclonal RPA1 Primary Antibody for ICC, FACS - ABIN969564
Sowd, Wang, Pretto, Chazin, Opresko: Replication protein A stimulates the Werner syndrome protein branch migration activity. in The Journal of biological chemistry 2009
Human Polyclonal RPA1 Primary Antibody for WB - ABIN658336
Smith, Krumpelbeck, Jegga, Prell, Matrka, Kappes, Greis, Ali, Meetei, Wells: The nuclear DEK interactome supports multi-functionality. in Proteins 2018
Study shows that the catalytic activity of the exosome subunit EXOSC10 contributes to the homologous recombination (HR) pathway by degrading damage-induced lncRNAs and maintaining RNA homeostasis at double-strand breaks (DSBs). Results identify RNA clearance at DSBs as a step in the HR pathway that is required for the assembly of RPA onto the resected ssDNA, which in turn is a prerequisite for controlled DNA resection.
The RPA is defective in DNA replication and cell cycle progression, it was shown to play a supporting role in nucleotide excision repair and recombination.
RPA serves to stimulate the primase activity of PrimPol.
Data show that short ssDNA traverses the nuclear membrane, but is drawn into the nucleus by binding to the DNA replication and repair factors replication protein A (RPA) and Rad51 recombinase (Rad51).
These new findings supports the existence of a functional PrimPol/RPA association that allows repriming at the exposed ssDNA regions formed in the leading strand upon replicase stalling.
regulatory pathway based on casein kinase 2-G9a-RPA permits homologous recombination in cancer cells
RPA1 serves as an oncogene during gastrointestinal cancers progression
RPA1 is significantly up-regulated in hepatocellular carcinoma and correlates with poor prognosis. RPA1 influences cell cycle through CDK4/Cyclin-D pathway.
PCAF/GCN5-mediated lysine 163 acetylation of RPA1 is crucial for nucleotide excision repair.
the acetylation status of RPA1 played a crucial role in repair of DNA damage via nucleotide excision repair.
data obtained allow us to suggest that XPA can be involved in the post-incision NER stages via its interaction with RPA
The results suggest that RPA phosphorylation enhances the recruitment of PRP19 to RPA-ssDNA and stimulates RPA ubiquitylation through a process requiring both PRP19 and RFWD3, thereby triggering a phosphorylation-ubiquitylation circuitry that promotes ATR activation and homologous recombination.
RPA recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation.
RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability.
Annealing helicase HARP closes RPA-stabilized DNA bubbles non-processively.
Architectural plasticity of human BRCA2-RPA-RAD51 complexes in DNA break repair has been described.
Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex.
Data suggest RAD52 binds tightly to RPA/ssDNA complex in presynaptic complex and inhibits RPA turnover; during presynaptic complex assembly, most of RPA and RAD52 is displaced from ssDNA, but some RAD52/RPA/ssDNA complexes persist as interspersed clusters surrounded by RAD51 filaments. (RAD52 = Rad52 DNA repair/recombination protein; RPA = replication protein A; ssDNA = single-stranded DNA; RAD51 = Rad51 recombinase)
Data suggest that, during human DNA replication, restricting PCNA (proliferating cell nuclear antigen) to the vicinity of its DNA target site is important; PCNA can be maintained at or near primer/template junctions during DNA synthesis by RPA (replication protein A) or SSB (single-stranded DNA-binding protein); here, the SSB used was from Escherichia coli.
Strikingly, the addition of the single-stranded DNA (ssDNA)-binding replication protein A (RPA) selectively restores XPF-ERCC1 endonuclease activity on this structure. The 5'-3' exonuclease SNM1A can load from the XPF-ERCC1-RPA-induced incisions and digest past the crosslink to quantitatively complete the unhooking reaction.
localization of the replication protein A (RPA) complex on the chromosome axes meiotic prophase in mouse spermatocytes, is reported.
Using an inducible germline-specific inactivation strategy, we find that loss of RPA completely abrogates loading of RAD51/DMC1 recombinases to programmed meiotic DNA double strand breaks, thus blocking strand invasion required for chromosome pairing and synapsis.
The recovery of abnormal phenotypes of mutant Ataxin-1 knock-in (Atxn1-KI) mice in the dendrite and spine morphology of Purkinje cells by AAV vector-mediated expression of RpA1 was reported.
The authors establish that a second Dna2-Rpa interaction is mutually exclusive with Rpa-DNA interactions and mediates the displacement of Rpa from ssDNA.
LT prevents recruitment of RPA to nuclear foci after DNA damage. This leads to failure to recruit repair proteins such as Rad51 or Rad9, explaining why LT prevents repair of double strand DNA breaks by homologous recombination.
Most RPA recruitment during class switch recombination represents salvage of unrepaired breaks by homology-based pathways during the S-G2/M phase of the cell cycle.
POT1a degradation resulted in rapid and reversible activation of the ATR pathway in G1 and S/G2.
Rpa1(L230P) missense mutation significantly alters the tumor phenotype and spectrum of Trp53 mutant mice by modifying the genetic mechanisms underlying tumorigenesis.
both TNFR-p55 and TNFR-p75 appear to be of minimal importance for modulation of Fas-mediated apoptosis and associated A1 protein expression despite normal Fas/TNFR-p55 and increased TNFR-p75 expression in neutrophils
Rpa1 functions in DNA metabolism are essential for the maintenance of chromosomal stability and tumor suppression.
hyperphosphorylation may play a role in modulating cellular pathways by altering the DNA binding domain-mediated RPA-DNA and RPA-protein interactions, hypothetically via the interaction of hyperphosphorylated RPA32N with DBD-B
These results demonstrate that neither RPA hyper-phosphorylation nor H2AX are required for the formation in RPA intra-nuclear foci in response to DNA damage/replicational stress.
This study found that the N-terminus of the RPA large subunit interacts with both WRN and DNA2 and is essential for stimulating WRN's 3'->5' helicase activity and DNA2's 5'->3' ss-DNA exonuclease activity.
The results provide strong biochemical evidence to link RPA to a specific DSB repair pathway and reveal a novel function of RPA in the generation of 3' ss-DNA for homology-dependent DSB repair.
Replication protein A accumulated increasingly on replication-arrested chromatin.
RPA1 subunit may directly recognize and bind to the 5-formyluracil on the single-stranded DNA.
loss-of-function alleles indicate that RPA is required to prevent neuroepithelial cells from differentiating into medulla neuroblasts
Data show that the basic cleft of the RPA70 N-terminal OB-fold domain binds multiple checkpoint proteins, including RAD9, to promote ATR signaling.
Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair\; it does not support chromosomal DNA replication and cell cycle progression through S- phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.
, RF-A protein 1
, RP-A p70
, replication factor A protein 1
, replication protein A 70 kDa DNA-binding subunit
, single-stranded DNA-binding protein
, replication protein A1, 70kDa
, replication protein A1
, replication protein A 70 kDa DNA-binding subunit-like
, replication protein A (RPA)
, drosophila replication protein A
, replication protein A 70
, single stranded-binding protein 70