Analytical Data
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Gene name
RPP25
- Application
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Alternative Names
(RNase P protein subunit p25)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BUL9
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Expression Region
1-199aa
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Molecular Weight
25.6 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
RPP25, or ribonuclease P protein subunit 25, is a critical component of the ribonuclease P complex, which plays a vital role in tRNA processing by catalyzing the cleavage of precursor tRNA molecules to generate mature tRNA. The study of RPP25, particularly its recombinant protein form, has garnered attention due to its essential functions in RNA metabolism and cellular processes. Understanding the structure and function of RPP25 can provide insights into RNA processing mechanisms and their implications in various biological systems. Moreover, the involvement of RPP25 in cellular stress responses and its potential connections to diseases such as cancer make it a target of interest for therapeutic research. The recombinant production of RPP25 allows for detailed biochemical and biophysical characterization, facilitating studies on its interactions with other protein and RNA components in the ribonuclease P complex. Through these investigations, researchers aim to elucidate the precise role of RPP25 in tRNA maturation and its broader implications in gene expression regulation and cellular homeostasis. The availability of this recombinant protein can also pave the way for drug development strategies aimed at modulating the activity of RNA processing enzymes, making RPP25 a significant focus in molecular biology and therapeutic research.
