RNASEH1 Antibody

Code CSB-PA019801GA01HU
Size $600
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Product Details

Uniprot No.
Target Names
RNASEH1
Alternative Names
RNASEH1 antibody; RNH1 antibody; Ribonuclease H1 antibody; RNase H1 antibody; EC 3.1.26.4 antibody; Ribonuclease H type II antibody
Raised in
Rabbit
Species Reactivity
Human,Mouse,Rat
Immunogen
Human RNASEH1
Immunogen Species
Homo sapiens (Human)
Isotype
IgG
Purification Method
Antigen Affinity purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
Tested Applications
ELISA,WB
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II.
Gene References into Functions
  1. RNASEH1 gene variants associate with susceptibility/protection to T1 Diabetes in Colombia. PMID: 29204916
  2. Studies indicate that ribonuclease H1 is essential for mitochondrial DNA replication. PMID: 27402764
  3. Data show that the catalytic domains of E. coli and human RNase H have nearly identical sequence preferences, which correlate with the efficiency of RNase H-recruiting antisense oligonucleotides. PMID: 29126318
  4. 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. PMID: 28717002
  5. RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. PMID: 28257700
  6. RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely PMID: 25330849
  7. found that the 3' fragments of target pre-mRNA generated by ASO were almost completely degraded from their 5' ends by nuclear XRN2 after RNase H1-mediated cleavage PMID: 26159921
  8. Altered RNaseH1 has a reduced capability to remove the RNA from RNA-DNA hybrids leading to impaired mtDNA replication and adult-onset mitochondrial encephalomyopathy. PMID: 26094573
  9. RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing PMID: 23990920
  10. 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 PMID: 23078533
  11. 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. PMID: 21443203
  12. Observational study of gene-disease association. (HuGE Navigator) PMID: 20877624
  13. The cysteine residues responsible for the redox-dependent activity of RNase H1 were determined by site-directed mutagenesis to involve Cys(147) and Cys(148), producing an inactive enzyme conformation by disulfide bond formation. PMID: 12473655
  14. Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate PMID: 14506260
  15. in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs PMID: 14960586
  16. analysis of catalytic site of human RNase H1 for heteroduplex substrate catalysis PMID: 15205459
  17. method for enhancing the human RNase H1 activity of chimeric antisense oligonucleotides PMID: 17028157
  18. THE role substrate structure plays in directing human RNase H1 activity as well as the design of effective antisense oligodeoxyribonucleotides. PMID: 17028158
  19. Report crystal structures of RNase H1 in complex with RNA/DNA hybrids. PMID: 17964265
  20. Characterization of full-length enzymes with defective hybrid binding domain indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1. PMID: 18337749

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Involvement in disease
Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 2 (PEOB2)
Subcellular Location
Cytoplasm.
Protein Families
RNase H family
Tissue Specificity
Ubiquitous.
Database Links

HGNC: 18466

OMIM: 604123

KEGG: hsa:246243

STRING: 9606.ENSP00000313350

UniGene: Hs.568006

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