Analytical Data
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Gene name
stxB2
- Application
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Alternative Names
stxB2；UNC18B；Syntaxin-binding Protein 2
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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
P09386
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Expression Region
20-89aa
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AA Sequence
ADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND
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Molecular Weight
14.7 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
The stxB2 recombinant protein is derived from the Shiga toxin-producing bacteria, specifically Escherichia coli. Shiga toxins are potent virulence factors associated with serious human diseases, such as hemolytic uremic syndrome (HUS) and hemorrhagic colitis. The stxB2 subunit plays a crucial role in the toxicity mechanism, facilitating the entry of the active A subunit into host cells by binding to glycolipids on the cell surface. Research on stxB2 has gained importance due to its potential implications in vaccine development and therapeutic interventions. Recombinant forms of this protein can be used to study the toxin's biological effects, elucidate its mechanisms of action, and serve as candidates for diagnostics or immunization strategies. Understanding the structure and function of stxB2 is essential for developing strategies to counteract the pathogenicity of Shiga toxin-producing E. coli strains and to mitigate their health impacts. Advances in recombinant DNA technology have enabled the production of stxB2 in sufficient quantities for extensive research, fostering collaborations across microbiology, immunology, and vaccine development sectors. As the global incidence of infections caused by Shiga toxin-producing E. coli remains a public health concern, the exploration of stxB2 recombinant protein continues to be a pivotal area of investigation aimed at reducing disease burden and enhancing food safety.
