Analytical Data
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Gene name
RNASEH2A
- Application
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Alternative Names
RNASEH2A;RNASEHI;RNHIA;Ribonuclease H2 subunit A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75792
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Expression Region
1-299aa
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AA Sequence
MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC YCPLPRLADL EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL ISTSMLGRVK YNLNSLSHDT ATGLIQYALD QGVNVTQVFV DTVGMPETYQ ARLQQSFPGI EVTVKAKADA LYPVVSAASI CAKVARDQAV KKWQFVEKLQ DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT AQTILEKEAE DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL
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Molecular Weight
33.3 kDa
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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
RNASEH2A is a crucial component of the ribonuclease H2 (RNase H2) complex, which plays a significant role in the DNA replication and repair processes by removing RNA moieties from RNA-DNA hybrids. Mutations in the RNASEH2A gene have been associated with a rare genetic disorder known as Aicardi-Goutières syndrome (AGS), which is characterized by neurodevelopmental defects and an autoimmune-like response. Understanding the structure and function of RNASEH2A is vital for elucidating its role in maintaining genomic stability and its implications in human diseases. Recent research focuses on the recombinant expression of RNASEH2A to investigate its biochemical properties, enzymatic function, and interaction with other proteins in the RNase H2 complex. This recombinant protein study aims to provide insights into its molecular mechanisms, highlight its potential as a therapeutic target, and contribute to the development of strategies for treating RNASEH2A-related disorders. By characterizing RNASEH2A, researchers can better understand not only its fundamental biological functions but also its broader implications in cellular processes and human health.











