Recombinant Human Ribonuclease H1 (RNASEH1)

In Stock
Code CSB-EP019801HU
MSDS
Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP019801HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RNASEH1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP019801HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RNASEH1.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
RNASEH1
Uniprot No.
Research Area
Epigenetics and Nuclear Signaling
Alternative Names
RNASEH1; RNH1; Ribonuclease H1; RNase H1; EC 3.1.26.4; Ribonuclease H type II
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
1-286aa
Target Protein Sequence
MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
37.6 kDa
Protein Length
Full Length
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Discover the power of precision with our Recombinant Human RNASEH1 protein, an essential tool for advancing research in epigenetics and nuclear signaling. Ribonuclease H1 (RNase H1; Ribonuclease H type II) is a critical enzyme involved in the removal of RNA:DNA hybrids formed during replication, transcription, and repair processes. RNASEH1 plays a pivotal role in maintaining genome stability and has been implicated in various biological pathways, making it an important target for scientific inquiry.

Our Recombinant Human RNASEH1 protein is expressed in E.coli, resulting in a full-length protein (1-286aa) that retains its native folding and function. The N-terminal 6xHis-tag allows for efficient purification, while the purity of the protein, greater than 85% as determined by SDS-PAGE, ensures consistent and reliable results for your research endeavors. Available in both liquid and lyophilized powder forms, our Recombinant Human RNASEH1 protein is the ideal choice for your epigenetic and nuclear signaling investigations.

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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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