Analytical Data
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Gene name
cdtB
- Application
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Alternative Names
Deoxyribonuclease CdtB (EC:3.1.-.-)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q46669
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Expression Region
19-269aa
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Molecular Weight
47.4 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
CdtB, a component of the cytolethal distending toxin (CDT) produced by certain pathogenic bacteria, has garnered significant attention in the field of microbiology and immunology due to its role in bacterial pathogenesis and its potential as a therapeutic target. This toxin is known to induce cell cycle arrest and promote apoptosis in host cells, which contributes to the virulence of bacteria such as *Campylobacter jejuni*, *Escherichia coli*, and *Helicobacter pylori*. Research into CdtB has revealed its mechanism of action, which involves the targeting of host cell DNA and disrupting cellular functions. Understanding the structure and function of CdtB is crucial for developing strategies to inhibit its activity, paving the way for novel therapeutic approaches against CDT-producing pathogens. Moreover, CdtB has been explored as a vaccine candidate, due to its ability to elicit immune responses, thus highlighting its dual role both as a virulence factor and a potential tool in immunotherapy. As studies continue to unravel the complexities of CdtB interactions with the host immune system, the insights gained may lead to advancements in vaccines and treatments for infectious diseases caused by CDT-producing bacteria, underscoring the importance of this research in combating bacterial infections effectively.
