Analytical Data
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Gene name
RPP14
- Application
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Alternative Names
RPP14; Ribonuclease P protein subunit p14; EC 3.1.26.5
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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
O95059
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Expression Region
2-124 aa
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AA Sequence
PAPAATYER VVYKNPSEYH YMKVCLEFQD CGVGLNAAQF KQLLISAVKD LFGEVDAALP LDILTYEEKT LSAILRICSS GLVKLWSSLT LLGSYKGKKC AFRVIQVSPF LLALSGNSRE LVLD
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Molecular Weight
13.6 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
RPP14, also known as ribonuclease P protein subunit 14, is a crucial component of the ribonuclease P (RNase P) complex, which plays an essential role in tRNA processing by cleaving precursor tRNA molecules to produce mature tRNAs. The study of RPP14 has gained significant attention due to its involvement in various cellular processes and its potential implications in disease states. Research has shown that RPP14 is not only vital for the enzymatic activity of RNase P but also plays a role in the stability and assembly of the ribonucleoprotein complex. Moreover, abnormalities in RPP14 expression and function have been linked to several disorders, including certain cancers and neurodegenerative diseases, making it a candidate for further investigation into therapeutic interventions. Understanding the structure-function relationship of RPP14, as well as its interactions with other protein and RNA components of the RNase P complex, is critical for elucidating its biological roles and potential regulatory mechanisms. As researchers aim to uncover the molecular pathways influenced by RPP14, its role in cellular metabolism and gene expression regulation presents promising avenues for both basic and applied research, including biotechnological applications and drug development. The continued exploration of RPP14 and its associated pathways may reveal novel insights into ribonucleoprotein functionality and its broader implications in health and disease.
