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Human Polyclonal POLH Primary Antibody pour WB - ABIN1882183
Glick, Vigna, Loeb: Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions. dans The EMBO journal 2001
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Human Polyclonal POLH Primary Antibody pour IP, WB - ABIN253042
Day, Palle, Barkley, Kakusho, Zou, Tateishi, Verreault, Masai, Vaziri: Phosphorylated Rad18 directs DNA polymerase η to sites of stalled replication. dans The Journal of cell biology 2010
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Error-free insertion in cyclobutane pyrimidine bypass is due mainly to pol eta (translesion synthesis TLS3) in oocyte extracts during DNA replication.
In human DNA polymerase eta, the conserved Arg61 favors Watson-Crick base pairing through defined interactions with the incoming nucleotide.
POLH & POLK (Montrer PAPD7 Anticorps) are both able to exchange with PolD1 (Montrer POLD1 Anticorps) stalled at repetitive CFS (common fragile sites) sequences. POLD1 (Montrer POLD1 Anticorps) synthesis was inhibited by replication stress caused by aphidicolin, preventing any replication past CFS. Importantly, POLH & POLK (Montrer PAPD7 Anticorps) were still proficient in rescuing this stalled POLD1 (Montrer POLD1 Anticorps) synthesis. POLD1 (Montrer POLD1 Anticorps) stalling at CFSs allows for free exchange with specialized polymerase that is not driven by PCNA (Montrer PCNA Anticorps).
Two novel mutations in the POLH gene, which encodes the translesion DNA polymerase eta, with loss of function due to two independent exon skippings, are reported to be associated as a compound heterozygous state in the patient.
Data suggest that DNA polymerase eta (POLH/RAD30) is able to bind DNA/DNA, RNA/DNA, and DNA/RNA duplexes with similar affinities; DNA polymerase eta (as well as DNA polymerase kappa (Montrer PAPD7 Anticorps)) accommodates RNA as one of the two strands during primer extension; both polymerases elongate RNA/DNA and DNA/RNA hybrids; additionally, DNA polymerase eta catalyzes reverse transcription.
POLH is phosphorylated by CDK2 (Montrer CDK2 Anticorps).POLH serine 687 is a CDK (Montrer CDK4 Anticorps) target and is regulated during the cell cycle.POLH phosphorylation controls protein stability.
The current work explores both the fidelity of DNA polymerase eta and the role of the 3rd metal ion (magnesium), by using empirical valence bond simulations.
The results suggest that translesion synthesis by Pol eta can contribute to the accumulation of rCMP in the genome, particularly opposite modified guanines.
the targeting of Poleta to damage sites after UV exposure is regulated by SPARTAN, and this function contributes highly to its DNA-damage tolerance function.
Study shows that the posttranslational modifications of nuclear localization signal of pol eta played a dual role in polymerase switching, where Lys682 deubiquitination promotes the recruitment of pol eta to PCNA (Montrer PCNA Anticorps) immediately prior to lesion bypass and Ser687 phosphorylation stimulates its departure from the replication fork immediately after lesion bypass.
The data directly show that, in the human genome, DNA Pol-eta and Rev1 bypass cyclobutane pyrimidine dimers and 6-4PP at replication forks, while only 6-4PP are also tolerated by a Rev3L-dependent gap-filling mechanism, independent of S phase.
the functions of REV3L in maintaining cell viability, embryonic viability and genomic stability are directly dependent on its polymerase activity, and cannot be ameliorated by an additional deletion of pol eta.
XP-V has a role in adipose tissue senescence and metabolic syndrome
Increase in UV-induced mutations at both G:C and A:T pairs associated with PolH deficiency suggests that PolH contributes to accurate translesion synthesis (TLS (Montrer FUS Anticorps)) past both T- & C-containing dimers.
POLH deficiency did not affect the frequency and patterns of C:G mutations and UNG (Montrer UNG Anticorps) POLH double deficiency showed an additive effect of single deficiency.
REV1 and Polkappa are involved in DNA damage tolerance via Poleta-REV1 interaction when Poleta fails to bypass its cognate substrates.
These results reveal genetic interactions between REV1 catalytic activity and POLH and identify an alternative pathway in the generation of C to G and G to C transversions.
these data support the existence of PCNA (Montrer PCNA Anticorps) ubiquitination-dependent and -independent activation pathways of Poleta during somatic hypermutation and DNA damage tolerance.
inaccurate DNA synthesis by mammalian DNA polymerase eta (pol eta) contributes to somatic hypermutation (SHM (Montrer CNTNAP1 Anticorps)) of Ig genes
suggest the involvement of the Pol eta and Pol iota (Montrer POLI Anticorps) proteins in UV-induced skin carcinogenesis
Results reveal genetic and biochemical interactions between DNA polymerases eta (POLH) and theta (POLQ (Montrer POLQ Anticorps)) and suggest that POLQ (Montrer POLQ Anticorps) might cooperate with POLH to generate some of the A/T mutations during the somatic hypermutation of Ig genes.
This gene encodes a member of the Y family of specialized DNA polymerases. It copies undamaged DNA with a lower fidelity than other DNA-directed polymerases. However, it accurately replicates UV-damaged DNA\; when thymine dimers are present, this polymerase inserts the complementary nucleotides in the newly synthesized DNA, thereby bypassing the lesion and suppressing the mutagenic effect of UV-induced DNA damage. This polymerase is thought to be involved in hypermutation during immunoglobulin class switch recombination. Mutations in this gene result in XPV, a variant type of xeroderma pigmentosum.
DNA-directed DNA polymerase eta
, DNA polymerase eta
, polymerase (DNA directed), eta
, DNA polymerase eta-like
, polymerase eta
, RAD30 homolog A
, xeroderma pigmentosum variant type protein
, polymerase (DNA directed), eta (RAD 30 related)
, xeroderma pigmentosum variant type protein homolog