Recombinant Human Ribonuclease H1 (RNASEH1) Protein (His)

Name: Recombinant Human Ribonuclease H1 (RNASEH1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02776P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RNASEH1.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ribonuclease H1 (RNASEH1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O60930
Target Symbol	RNASEH1
Synonyms	RNASEH1; RNH1; Ribonuclease H1; RNase H1; EC 3.1.26.4; Ribonuclease H type II
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
Expression Range	1-286aa
Protein Length	Full Length
Mol. Weight	37.6 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm.
Protein Families	RNase H family
Database References	HGNC: 18466 OMIM: 604123 KEGG: hsa:246243 STRING: 9606.ENSP00000313350 UniGene: Hs.568006
Associated Diseases	Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 2 (PEOB2)
Tissue Specificity	Ubiquitous.

Gene Functions References

RNASEH1 gene variants associate with susceptibility/protection to T1 Diabetes in Colombia. PMID: 29204916
Studies indicate that ribonuclease H1 is essential for mitochondrial DNA replication. PMID: 27402764
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
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
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
RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely PMID: 25330849
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
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
RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing PMID: 23990920
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
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
Observational study of gene-disease association. (HuGE Navigator) PMID: 20877624
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
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
in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs PMID: 14960586
analysis of catalytic site of human RNase H1 for heteroduplex substrate catalysis PMID: 15205459
method for enhancing the human RNase H1 activity of chimeric antisense oligonucleotides PMID: 17028157
THE role substrate structure plays in directing human RNase H1 activity as well as the design of effective antisense oligodeoxyribonucleotides. PMID: 17028158
Report crystal structures of RNase H1 in complex with RNA/DNA hybrids. PMID: 17964265
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.