Analytical Data
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Gene name
DTNb
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60941
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Expression Region
Met1~Glu249
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Molecular Weight
33kDa
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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
DTNb, or Diphtheria Toxin-Nontoxic Binary Protein, is an engineered protein derived from the diphtheria toxin's structure with modifications that render it non-toxic while retaining its ability to bind to cells. This research has gained traction due to the potential applications of DTNb in targeted drug delivery and immunotherapy. The interest in DTNb stems from the need for more effective therapeutic strategies, particularly in cancer treatment, where conventional methods can result in significant side effects and systemic toxicity. By utilizing DTNb's ability to specifically target and enter cells, researchers aim to develop innovative treatments that can deliver therapeutic agents directly to diseased cells, thus minimizing damage to healthy tissues. Furthermore, studies have explored the fusion of DTNb with various effector domains, enhancing its therapeutic efficacy. This protein's modular nature allows it to be fine-tuned for specific applications, making it a promising candidate in the ever-evolving field of biomedicine. Overall, the research into DTNb not only highlights its potential utility in disease treatment but also underscores the importance of engineered proteins in advancing medical interventions.
