Analytical Data
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Gene name
eltB
- Application
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Alternative Names
eltB；Heat-labile enterotoxin B chain
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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
P32890
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Expression Region
22-124aa
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AA Sequence
APQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKN
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Molecular Weight
19.2 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 study of the eltB recombinant protein is grounded in its significant role in microbial pathogenesis and biotechnological applications. eltB, derived from certain pathogenic bacteria, encodes for components that can impact virulence and resistance, making it a vital target for understanding disease mechanisms and developing novel therapeutic strategies. Researchers are particularly interested in its potential applications in vaccine development, as the recombinant form can elicit robust immune responses without the risks associated with live pathogens. Additionally, eltB serves as a model for studying protein expression and purification techniques, offering insights into protein folding, stability, and activity. This research is crucial not only for advancing our knowledge of bacterial infections but also for harnessing the protein's properties in industrial and healthcare settings, paving the way for innovations in diagnostics and treatment protocols. The elucidation of eltB’s structure-function relationship remains a focal point, thus driving ongoing investigations into its biochemical properties and interactions within biological systems.
