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Endonuclease that specifically degrades the RNA of RNA- DNA hybrids.. Additionally we are shipping Ribonuclease H1 Proteins (6) and many more products for this protein.
Showing 10 out of 27 products:
Cow (Bovine) Polyclonal RNASEH1 Primary Antibody for WB - ABIN2778825
Nowotny, Cerritelli, Ghirlando, Gaidamakov, Crouch, Yang: Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD. in The EMBO journal 2008
Human Polyclonal RNASEH1 Primary Antibody for IHC, IHC (p) - ABIN4350680
Tresini, Warmerdam, Kolovos, Snijder, Vrouwe, Demmers, van IJcken, Grosveld, Medema, Hoeijmakers, Mullenders, Vermeulen, Marteijn: The core spliceosome as target and effector of non-canonical ATM signalling. in Nature 2015
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
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 Antibodies) 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 Antibodies)(147) and Cys (show DNAJC5 Antibodies)(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
in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs
analysis of catalytic site of human RNase H1 for heteroduplex substrate catalysis
Endonuclease that specifically degrades the RNA of RNA- DNA hybrids.
, ribonuclease H1
, ribonuclease H1 pseudogene 1
, Ribonuclease H1
, RNase H1
, ribonuclease H type II