Analytical Data
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Gene name
RPP25
- Application
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Alternative Names
RPP25；Ribonuclease P Protein subunit p25
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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
Q9BUL9
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Expression Region
1-199aa
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AA Sequence
MENFRKVRSEEAPAGCGAEGGGPGSGPFADLAPGAVHMRVKEGSKIRNLMAFATASMAQPATRAIVFSGCGRATTKTVTCAEILKRRLAGLHQVTRLRYRSVREVWQSLPPGPTQGQTPGEPAASLSVLKNVPGLAILLSKDALDPRQPGYQPPNPHPGPSSPPAAPASKRSLGEPAAGEGSAKRSQPEPGVADEDQTA
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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, short for ribonuclease P protein subunit 25, is a crucial component of the ribonuclease P complex, which is responsible for the maturation of tRNA by cleaving its precursor molecules. This protein plays a pivotal role in the cleaving process, not only participating in the enzymatic activity but also contributing to the stability and functionality of the RNase P complex. Research on RPP25 has garnered interest due to its essential function in RNA processing and its potential implications in various biological processes and diseases. Studies have shown that dysregulation of RPP25 may lead to impaired tRNA processing, which can affect protein synthesis and cellular function. Additionally, its involvement in RNA-related pathways has suggested a link between RPP25 and various cellular stress responses. Understanding the structure, function, and interactions of RPP25 can provide valuable insights into its role in cellular homeostasis and its potential as a therapeutic target. Recent advances in recombinant protein technology have facilitated the production and study of RPP25, allowing researchers to investigate its biochemical properties and interactions with other components of the RNase P complex. This has opened new avenues for exploring the functional implications of RPP25 in both normal cellular physiology and pathological states, thus highlighting the importance of this protein in the broader context of molecular biology and medicine.
