Analytical Data
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基因名
D15
- Application
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别名
exo5
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种属
Others
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P06229
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表达区间
M1-Q291
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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
Related Products
Protein Description
The D15 recombinant protein has garnered significant attention in the field of biochemistry and molecular biology due to its potential applications in vaccine development and therapeutic interventions. This protein is derived from the D15 antigen, which is associated with certain pathogenic microorganisms. Previous studies have highlighted its role in eliciting an immune response, making it a candidate for further exploration in immunotherapy and vaccine formulation. Researchers are particularly interested in D15 because of its ability to induce both humoral and cellular immunity, which are critical for an effective immune response. The recombinant production of D15 utilizes advanced genetic engineering techniques, allowing for its purification and characterization in controlled laboratory settings. This approach not only improves the yield of the protein but also enhances its stability and efficacy. As global health challenges continue to evolve, particularly with emerging infectious diseases, the development of robust vaccines incorporating D15 recombinant protein could provide a strategic advantage in immunization efforts. Ongoing investigations are focused on optimizing the immunogenicity of this protein and understanding its mechanisms of action within the immune system. Through these research initiatives, the D15 recombinant protein stands at the forefront of translational research, with the potential to significantly impact public health by enabling the design of novel vaccines and therapeutic strategies against various infectious agents.












