Analytical Data
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Gene name
RNASEH1
- Application
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Alternative Names
Rnase-H; RNASEH1; RNH1; Ribonuclease H type II
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60930
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Expression Region
Met1~Asp286
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Molecular Weight
62kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
RNASEH1 (Ribonuclease H1) is an essential enzyme that plays a critical role in the processing of RNA during DNA replication and repair. It specifically degrades the RNA strand of RNA-DNA hybrids, which are formed during DNA replication, thus facilitating the removal of RNA primers and ensuring the fidelity of DNA synthesis. Mutations in the RNASEH1 gene have been linked to various genetic disorders, including mitochondrial diseases, underscoring its importance in maintaining genomic stability. The study of RNASEH1 recombinant proteins has gained significant attention as researchers aim to understand its mechanism of action and regulatory functions in cellular processes. By producing RNASEH1 in a recombinant form, scientists can investigate its enzymatic activity, structure-function relationships, and interactions with other molecular partners. Understanding these aspects is crucial, as it could pave the way for developing therapeutic strategies targeting RNASEH1-related diseases and enhancing our knowledge of fundamental biological processes involving RNA metabolism and DNA repair. Consequently, the exploration of RNASEH1 recombinant proteins serves as a vital component in molecular biology, biotechnology, and therapeutic development, with promising implications for treating conditions associated with RNASEH1 dysfunction.
