Analytical Data
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Gene name
POP7
- Application
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Alternative Names
Ribonucleases P/MRP protein subunit POP7 homolog
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75817
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Expression Region
1-140aa
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Molecular Weight
42.7 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
POP7, a key component of the ribonuclease P (RNase P) complex, has garnered significant attention in molecular biology due to its critical role in tRNA processing and maturation in eukaryotic cells. As an essential enzyme, RNase P catalyzes the 5' maturation of precursor tRNA molecules, thereby playing a vital part in protein synthesis and overall cellular function. Research into POP7's recombinant protein has been motivated by its potential implications in various biological processes and diseases, including its involvement in the regulation of RNA metabolism and gene expression. Moreover, understanding POP7 and the RNase P complex could unveil novel therapeutic targets for RNA-related disorders and contribute to advancements in synthetic biology, where engineered RNase P could be utilized for targeted RNA processing applications. The study of POP7’s structure and function through recombinant protein techniques provides insights into enzyme mechanics and interactions within the RNase P complex, ultimately enhancing our understanding of ribonucleoprotein function and its impact on cellular health. As a result, the investigation of POP7 as a recombinant protein has significant implications for both fundamental biology and potential clinical applications.
