Analytical Data
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Gene name
RNASEH2B
- Application
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Alternative Names
RNASEH2B; DLEU8; Ribonuclease H2 subunit B; RNase H2 subunit B; Aicardi-Goutieres syndrome 2 protein; AGS2; Deleted in lymphocytic leukemia 8; Ribonuclease HI subunit B
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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
Q5TBB1
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Expression Region
2-312 aa
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AA Sequence
AAGVDCGDG VGARQHVFLV SEYLKDASKK MKNGLMFVKL VNPCSGEGAI YLFNMCLQQL FEVKVFKEKH HSWFINQSVQ SGGLLHFATP VDPLFLLLHY LIKADKEGKF QPLDQVVVDN VFPNCILLLK LPGLEKLLHH VTEEKGNPEI DNKKYYKYSK EKTLKWLEKK VNQTVAALKT NNVNVSSRVQ STAFFSGDQA STDKEEDYIR YAHGLISDYI PKELSDDLSK YLKLPEPSAS LPNPPSKKIK LSDEPVEAKE DYTKFNTKDL KTEKKNSKMT AAQKALAKVD KSGMKSIDTF FGVKNKKKIG KV
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Molecular Weight
35.1 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
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Protein Description
RNASEH2B is a crucial enzyme involved in RNA metabolism, specifically in the degradation of ribonucleic acid (RNA) strands that are hybrids with deoxyribonucleic acid (DNA). Dysfunction of RNASEH2B has been linked to a variety of human diseases, notably autoimmune disorders and neurodegenerative conditions. Research has shown that mutations in the RNASEH2B gene can lead to Aicardi-Goutières syndrome, a severe neuroinflammatory disorder that manifests in infancy and is characterized by features reminiscent of congenital infections. Given the enzyme's role in maintaining genomic stability and regulating p53 signaling, understanding its function and mechanism is critical for developing targeted therapies for associated disorders. Recent studies have focused on generating recombinant RNASEH2B proteins to elucidate their structural and functional properties, examining how specific mutations affect enzyme activity, substrate binding, and interactions with other cellular components. These investigations not only enhance our knowledge of RNA-DNA hybrid metabolism but also guide potential therapeutic interventions for diseases arising from RNASEH2B dysfunction. The advancement in recombinant protein technology enables detailed analysis of RNASEH2B, offering insights into its catalytic mechanism and implications in cellular processes such as DNA repair and immune response, thus illuminating the broader significance of maintaining RNA-DNA homeostasis in cellular health and disease.
