Analytical Data
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Gene name
PRND
- Application
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Alternative Names
Prnd; Prion-like protein doppel; Doppelganger; Dpl; PrPLP
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Species
Mouse
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9QUG3
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Expression Region
27-155aa
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Molecular Weight
18.9 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
PRND (prion protein-like protein D) is a protein that has garnered attention in prion research due to its structural similarities to the normal prion protein (PrP). A member of the prion protein gene family, PRND plays a potential role in modulating prion diseases, which are neurodegenerative disorders characterized by misfolded proteins. Studies suggest that PRND may have a protective function against the pathogenic effects of abnormal prion protein conformations, thereby influencing the transmission and progression of prion-related diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. The investigation of PRND has opened up new avenues for understanding the mechanisms of prion diseases, including its interactions with PrP and other cellular factors. Furthermore, the exploration of PRND's expression patterns in different tissues and its evolutionary conservation across species offers insights into its biological significance. As researchers continue to decipher the role of PRND in prion pathology, this could lead to novel therapeutic strategies aimed at preventing or mitigating the effects of prion diseases, highlighting the importance of PRND in both basic science and clinical applications.
