Analytical Data
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Gene name
ystB
- Application
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Alternative Names
Y-STB
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Species
Yersinia enterocolitica
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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
P74977
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Expression Region
53-71aa
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Molecular Weight
18.1 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
YstB is a protein that has garnered attention in the field of molecular biology due to its potential role in various biochemical processes. It is a member of the Yersinia family, specifically associated with the pathogenic bacterium Yersinia pestis, which is known for causing plague. Understanding YstB's function and structure is crucial, as it may contribute to the virulence of this pathogen. Recent studies have aimed at producing recombinant YstB proteins to investigate their biochemical properties and interactions with host systems. This research is significant not only for elucidating the mechanisms of Yersinia pathogenesis but also for developing potential therapeutic strategies against infections caused by this bacterium. Recombinant protein technology allows for the generation of large amounts of YstB, facilitating detailed structural and functional analyses. As a result, researchers are focusing on characterizing the protein through techniques such as X-ray crystallography and mass spectrometry, aimed at determining its three-dimensional structure and interactions with other molecules. Additionally, the investigation extends to understanding how YstB affects host immune responses and the potential for it to serve as a biomarker or target for vaccines. Overall, the study of YstB recombination proteins represents a promising avenue for advancing our knowledge of microbial pathogenesis and developing innovative solutions to combat infectious diseases linked to Yersinia.
