Analytical Data
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Gene name
stxB
- Application
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Alternative Names
stxB；Syntaxin-binding Protein 4
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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
P69179
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Expression Region
21-89aa
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AA Sequence
TPDCVTGKVEYTKYNDDDTFTVKVGDKELFTNRWNLQSLLLSAQITGMTVTIKTNACHNGGGFSEVIFR
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Molecular Weight
13.3 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
The stxB recombinant protein is derived from the Shiga toxin B (StxB) subunit, which is produced by Shiga toxin-producing Escherichia coli (STEC), a significant pathogenic bacterium associated with severe gastrointestinal diseases. Research on stxB has gained prominence due to its role in the pathogenesis of STEC infections, particularly in the development of hemolytic uremic syndrome (HUS), a life-threatening condition. Understanding the structure and function of StxB is critical, as it facilitates the binding of the toxic A subunit to host cells, thereby enabling toxin entry and subsequent cellular disruption. The recombinant form of StxB is being studied for its potential applications in vaccine development and as a therapeutic agent to mitigate the effects of STEC infections. Additionally, stxB recombinant protein can serve as a useful tool in studying cellular signaling pathways and immune responses, paving the way for novel intervention strategies. The production of stxB in heterologous systems allows for detailed characterization and large-scale availability for research purposes. Consequently, it holds promise not only for advancing our understanding of STEC-induced diseases but also for developing effective preventative measures against this pressing public health issue.
