Analytical Data
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Gene name
PRNP
- Application
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Alternative Names
PRNP;ALTPRP;PRIP;PRP;Major prion Protein
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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
P04273
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Expression Region
23-231aa
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AA Sequence
KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS
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Molecular Weight
30.3 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
Related Products
Protein Description
The study of the prion protein gene (PRNP) recombinant protein has garnered significant attention in the field of molecular biology and neurodegenerative diseases, particularly in relation to prion diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. PRNP encodes the cellular prion protein (PrP), which exists in a primarily α-helical structure under normal conditions but can misfold into a pathogenic form, leading to neurodegeneration. Understanding the structural and functional characteristics of PRP is crucial for unraveling the mechanisms underlying prion propagation and pathogenesis. Recombinant PRNP proteins allow researchers to investigate the conformational changes, interactions with other cellular components, and the influence of mutations associated with prion diseases. These studies are essential for developing potential therapeutic strategies and diagnostic tools. Additionally, the production of recombinant PRNP enables the exploration of its role in normal physiology, immune response, and cellular signaling processes. Overall, ongoing research on PRNP recombinant protein represents a vital intersection of protein biochemistry, neurobiology, and therapeutic innovation, aiming to combat the devastating effects of prion-related disorders.
