Analytical Data
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基因名
DTNb
- Application
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O60941
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表达区间
Met1~Glu249
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分子量
33kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












