Analytical Data
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Gene name
ypr-10
- Application
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Alternative Names
ypr-10；Class 10 plant pathogenesis-related Protein 2B
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Species
E.coli
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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
D1YSM5
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Expression Region
1-157aa
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AA Sequence
MGAITYDMEIPSSISAEKMFKAFVLDGDTIIPKALPHAITGVQTLEGDGGVGTIKLTTFGEGSVHKSVKHRIDGLDKENFTYSYSIIEGGALDVFESISYHIKIVATPDGGCICKNRSIYTPKCDAQVSEEEIKAGKERASGIFKKVEAYLLANPDC
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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, a recombinant protein, has garnered significant attention in biochemical and pharmaceutical research due to its potential applications in various fields, including drug discovery and therapeutic development. As a member of a specific protein family, YPR-10 is believed to play a crucial role in cellular processes such as signal transduction, protein interactions, and metabolic regulation. Initial studies have indicated that YPR-10 exhibits unique structural characteristics that may enhance its functionality and stability as a recombinant product. Researchers are particularly interested in its implications for understanding disease mechanisms, especially in conditions where signaling pathways are disrupted. The recombinant production of YPR-10 allows for a controlled study of its properties, offering insights into its biological activities and interactions with other cellular components. Recently, advancements in molecular cloning, expression systems, and purification techniques have facilitated more efficient production of YPR-10, paving the way for in-depth research. Investigating YPR-10 can potentially lead to novel therapeutic strategies, particularly in the context of diseases where traditional treatments have proven inadequate. Overall, the study of YPR-10 as a recombinant protein holds promise for enhancing our understanding of complex biological systems and developing innovative solutions in medical science.
