Analytical Data
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Gene name
PRNP/CD230
- Application
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Alternative Names
CD230; GSS; ASCR; CJD; PRIP; PrP; PrP2730; PrPc; Major prion protein; Creutzfeldt-Jakob Disease; Gerstmann-Strausler-Scheinker Syndrome; Fatal Familial Insomnia
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Species
Rat
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13852
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Expression Region
29-231aa
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Molecular Weight
26.3 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
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Protein Description
PRNP (prion protein gene) encodes the prion protein, which is crucial in the study of prion diseases, a group of neurodegenerative disorders characterized by misfolded proteins leading to brain damage. The investigation of PRNP and its interactions has significant implications for understanding the pathogenesis of diseases such as Creutzfeldt-Jakob disease and fetal goat scrapie. CD230, also known as prion protein, has been identified as a key player in cellular functions, including cell signaling and interaction with other proteins. Research on PRNP/CD230 recombinant proteins aims to elucidate their structural properties, folding mechanisms, and the impact of specific mutations associated with prion diseases. By producing these recombinant proteins, scientists can conduct in vitro studies to analyze their behavior in real-time, investigate receptor binding, and explore potential therapeutic strategies to counteract prion-induced neurodegeneration. This research not only enhances our comprehension of protein misfolding and aggregation but also aids in the development of diagnostic tools and therapeutic interventions for prion diseases, thereby contributing significantly to the fields of neurobiology and regenerative medicine.
