Analytical Data
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Gene name
ypr-10
- Application
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Alternative Names
/
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Species
Actinidia deliciosa
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
D1YSM5
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Expression Region
1-157aa
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Molecular Weight
32.9 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
YPR-10 is a recombinant protein that has garnered significant interest in the field of biochemistry and molecular biology due to its potential applications in various research and therapeutic domains. Initially identified through genomic studies, YPR-10 is believed to play a crucial role in cellular processes such as signal transduction and protein-protein interactions. Its unique structural properties and functional domains make it an attractive candidate for further investigation. The study of YPR-10 aims to elucidate its biological functions and mechanisms of action, which may reveal insights into critical pathways associated with diseases, including cancer and metabolic disorders. Researchers aim to produce YPR-10 using recombinant DNA technology, allowing for high yields and purity essential for downstream applications, such as antibody production and functional assays. Furthermore, by investigating the binding affinities and interactions of YPR-10 with other cellular proteins, scientists hope to map out its role in various signaling networks. The findings from YPR-10 research could pave the way for novel therapeutic strategies, ultimately contributing to advancements in biomedical sciences and drug development. Understanding the complexities of YPR-10 may also provide a model for studying similar proteins in other organisms, thereby enhancing our knowledge of evolutionary biology and protein functionality.
