Analytical Data
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基因名
Ecotin
- Application
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种属
Escherichia coli O127:H6
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
B7UFM3
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表达区间
21-162aa
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分子量
23.5 kDa
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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
Ecotin is a protein originally derived from the bacterium *E. coli*, known for its ability to inhibit a wide range of serine proteases, including trypsin and chymotrypsin. Its unique structure and mechanism of action have made it a subject of interest in various fields, including biochemistry, pharmacology, and biotechnology. The research background of Ecotin centers on its potential applications in therapeutic settings, particularly due to its stability and effectiveness in various conditions. Scientists have explored the recombinant expression of Ecotin to produce it in larger quantities for functional studies, allowing for detailed analysis of its interaction with proteases and other proteins. By engineering Ecotin variants, researchers aim to enhance its inhibitory properties or develop novel functions for use in drug development or enzyme regulation. Additionally, Ecotin's role as a model system provides insights into protein folding, stability, and the dynamics of enzyme-inhibitor interactions, making it a valuable asset for both basic and applied research in protein science. Overall, the study of recombinant Ecotin offers promising avenues for advancing our understanding of protein interactions and developing new therapeutic agents.
