Analytical Data
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基因名
D13
- Application
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别名
D13
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种属
Virus
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表达系统
E. coli
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标签
Strep;His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
YP_010377107.1
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表达区间
M1-N551
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蛋白长度
Full Length
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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
The study of D13 recombinant protein has emerged as a significant area of interest within the field of molecular biology and protein engineering, particularly due to its potential applications in therapeutic and diagnostic contexts. D13 protein, a variant derived from a specific pathogen or mammalian source, has been shown to possess unique structural and functional characteristics that make it a promising candidate for various biomedical applications. Researchers are investigating the protein's role in immune response modulation, pathogen inhibition, and as a potential vaccine component. The development of recombinant D13 protein involves advanced genetic engineering techniques, allowing for the production of this protein in host organisms such as bacteria or yeast, which simplifies its purification and increases yield. Moreover, studies have demonstrated that modifications to the D13 protein can enhance its stability and activity, further broadening its applicability. The scientific community is keenly focused on elucidating the molecular mechanisms behind D13’s functions and interactions, aiming to harness these properties for innovative healthcare solutions. As a result, D13 recombinant protein research has the potential to contribute significantly to advancements in immunotherapy, vaccine development, and the creation of novel diagnostic tools, ultimately improving health outcomes in various disease contexts.
