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Endonuclease that specifically degrades the RNA of RNA- DNA hybrids.. Additionally we are shipping Ribonuclease H1 Antibodies (27) and many more products for this protein.
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Data suggest that ribonuclease H1 (RNASEH1) plays important role in replication fork movement by resolving R-loops (RNA-DNA hybrids); RNASEH1 depletion results in accumulation of RNA-DNA hybrids, slowing of replication forks, and increased DNA damage; RNASEH1 appears to contribute to genome stability and preserves telomere integrity.
RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability.
RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely
found that the 3' fragments of target pre-mRNA generated by ASO were almost completely degraded from their 5' ends by nuclear XRN2 (show XRN2 Proteins) after RNase H1-mediated cleavage
Altered RNaseH1 has a reduced capability to remove the RNA from RNA-DNA hybrids leading to impaired mtDNA replication and adult-onset mitochondrial encephalomyopathy.
RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing
data implicate the H264 side chain in phosphodiester hydrolysis as well as in product release, and are consistent with a proposed model in which the RNAse H1 H264 side chain interacts with a divalent metal ion to support catalysis
On the basis of its nuclear magnetic resonance (NMR) nucleic acid structure, a boranophosphonate-modified, fully R(P) BH(3) DNA/RNA hybrid is predicted not to be a substrate for RNase H1.
The cysteine residues responsible for the redox-dependent activity of RNase H1 were determined by site-directed mutagenesis to involve Cys (show DNAJC5 Proteins)(147) and Cys (show DNAJC5 Proteins)(148), producing an inactive enzyme conformation by disulfide bond formation.
Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate
RNase H1 is necessary for the activity of DNA-like ASOs. During liver regeneration, a clone of hepatocytes that expressed RNase H1 developed and partially restored mitochondrial and liver function.
the essential role of RNase H1 in mitochondrial DNA replication is the removal of primers at the origin of replication
translational organization of RNase H1 allows tight control of expression of RNase H1 in mitochondria, where its excess or absence can lead to cell death, without affecting the expression of the nuclear RNase H1
RNase H1 is involved in generation of mitochondrial DNA
Endonuclease that specifically degrades the RNA of RNA- DNA hybrids.
, ribonuclease H type II
, ribonuclease H1 pseudogene 1
, ribonuclease H1
, Ribonuclease H1