Analytical Data
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Gene name
RNASEP
- Application
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Alternative Names
RNASEP；Ribonuclease P Protein subunit p38
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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
P78346
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Expression Region
2-268aa
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AA Sequence
AVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG IISTVKKPRP SEGDEDCLPA SKKAKCEG
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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
RNASEP (Ribonuclease A Superfamily Protein) is a member of the ribonuclease A superfamily, known for its ribonucleolytic activity and involvement in various biological processes, including RNA metabolism, apoptosis, and immune responses. The interest in RNASEP has surged due to its potential applications in therapeutics and biotechnology. Research has shown that recombinant forms of RNASEP can be engineered to enhance their enzymatic properties or target specific RNA molecules, making them valuable tools in molecular biology and medicine. Moreover, RNASEP's ability to selectively degrade RNA has garnered attention for its implications in RNA-based therapies, including viral infections and cancer treatments, where modulating RNA levels can impact disease progression. Understanding the structure-function relationship of RNASEP through recombinant engineering can pave the way for the development of novel therapeutic strategies and innovative biotechnological applications, emphasizing its significance in both fundamental research and clinical applications. Continued investigation into RNASEP and its variants may lead to breakthroughs in understanding RNA biology and the development of RNA-targeted therapeutics.
