Analytical Data
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Gene name
PRND
- Application
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Alternative Names
PRND;DPL;Prion-like Protein doppel
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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
Q9UKY0
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Expression Region
27-152aa
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AA Sequence
TRGIKHRIKWNRKALPSTAQITEAQVAENRPGAFIKQGRKLDIDFGAEGNRYYEANYWQFPDGIHYNGCSEANVTKEAFVTGCINATQAANQGEFQKPDNKLHQQVLWRLVQELCSLKHCEFWLERG
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Molecular Weight
17 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 Doppel) is a protein that has garnered significant attention in recent years due to its intriguing role in prion diseases and neurodegenerative conditions. Originally identified as a homologue of the prion protein (PrP), which is implicated in various transmissible spongiform encephalopathies (TSEs), PRND’s function remains less understood. Research has shown that PRND may possess neuroprotective properties and may modulate the pathogenic effects of PrP, suggesting a complex interaction between these proteins. Increased levels of PRND have been observed in certain neurodegenerative diseases, leading scientists to investigate its potential as a biomarker or therapeutic target. Studies have also explored the structural characteristics of PRND, uncovering its unique features compared to PrP, such as differences in glycosylation and folding patterns. Understanding the precise mechanisms by which PRND operates could shed light on its role in neurological health and disease, and might open new avenues for treatment strategies aimed at prion-related disorders. The exploration of PRND's interactions with other cellular proteins and its potential neuroprotective effects could provide important insights into the pathogenesis of neurodegeneration, ultimately fostering the development of novel therapeutic approaches. Hence, PRND is a significant focus of ongoing research, with the goal of elucidating its biological functions and therapeutic potential in the context of prion diseases and broader neurodegenerative processes.
