Analytical Data
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Gene name
yst
- Application
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Alternative Names
yst; Heat-stable enterotoxin
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Species
Yersinia kristensenii
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31518
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Expression Region
51-66aa
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Molecular Weight
17.1 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
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Protein Description
YST recombinant proteins, derived from the Yersinia species, have garnered significant attention in the field of molecular biology and biotechnology due to their unique properties and potential applications. Yersinia, a genus of bacteria known for causing diseases such as the plague, possesses a range of proteins that play crucial roles in its pathogenicity. Researchers have focused on understanding the structure and function of these proteins to develop novel therapeutic strategies, vaccines, and diagnostic tools. The recombinant expression of YST proteins allows for detailed studies of their biochemical properties, interactions, and functionalities. By employing sophisticated techniques such as genetic engineering and protein purification, scientists aim to elucidate the mechanisms underlying Yersinia infections and to harness these proteins for biotechnological applications, including drug development and bioengineering. The exploration of YST recombinant proteins is crucial not only for advancing our understanding of bacterial pathogenesis but also for contributing to public health initiatives by providing new avenues for disease prevention and control.
