Analytical Data
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Gene name
RNU2
- Application
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Alternative Names
RNU2; Ribonuclease U2; RNase U2; EC 4.6.1.20
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Species
Ustilago sphaerogena
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Source
E. coli
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Tag
N- His-B2M
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00654
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Expression Region
1-114aa
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Molecular Weight
26.4 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
RNU2, a member of the small nuclear RNA (snRNA) family, plays a crucial role in the splicing of pre-mRNA within the spliceosome, a large RNA-protein complex that is essential for the proper processing of gene transcripts. The research on RNU2 recombinant protein has gained importance due to its potential implications in understanding the fundamental mechanisms of gene expression regulation and its association with various diseases, including cancer and neurological disorders. As snRNAs are vital for the synthesis of spliceosomal snRNPs (small nuclear ribonucleoproteins), the characterization of RNU2 recombinant protein can provide insights into RNA processing and cellular functions. Studies have shown that aberrations in snRNA processing, including RNU2, can lead to misregulated splicing, contributing to the pathogenesis of multiple diseases. Additionally, RNU2 recombinant protein can serve as a valuable tool for developing therapeutic strategies, such as targeting splicing machinery or designing RNA-based therapies. Efforts to express and purify RNU2 in a recombinant form have enabled researchers to investigate its structural and functional properties, further elucidating its role in the spliceosome dynamics and RNA metabolism. Understanding RNU2's biological significance and mechanistic pathways may offer new avenues for therapeutic interventions and enhance our grasp of the molecular underpinnings of splicing-related diseases. Overall, the study of RNU2 recombinant protein not only enriches our knowledge of RNA biology but also has the potential to contribute to the development of novel diagnostic and therapeutic approaches.
