Analytical Data
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基因名
SA
- Application
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种属
Pan-species (General)
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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
P22629
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表达区间
Asp25~Gln183
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分子量
18&84kDa
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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 SA (Streptavidin-Avidin) recombinant proteins originates from the need for high-affinity binding applications in molecular biology and biotechnology. Streptavidin, a protein derived from the bacterium *Streptomyces avidinii*, has a strong and specific affinity for biotin, a vitamin that plays a crucial role in cell metabolism. This exceptional binding strength has led to its widespread use in various applications, including protein purification, detection assays, and targeted drug delivery systems. The ability to produce recombinant forms of streptavidin enhances its utility by allowing researchers to modify the protein for specific purposes, such as improving binding kinetics, enhancing stability, or attaching other functional molecules. Additionally, the use of recombinant technology enables the production of streptavidin in large quantities and in a controlled environment, ensuring consistency and reliability in experimental outcomes. This has opened new avenues in the development of advanced diagnostic tools, biosensors, and therapeutic strategies, making SA recombinant proteins an important focus of ongoing research in both fundamental and applied sciences. Through this work, scientists are advancing our understanding of protein interactions and finding innovative solutions to complex biological problems.












