Analytical Data
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基因名
modA
- Application
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别名
(Molybdate/tungstate-binding protein ModA)
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P37329
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表达区间
25-257aa
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分子量
37.9 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
ModA is a significant protein involved in the transportation and sensing of various ligands, particularly in bacteria. Initially identified in prokaryotic organisms, ModA proteins are known for their role as periplasmic binding proteins, which facilitate the uptake of nutrients and signals from the environment. The study of ModA recombinant proteins has gained attention due to their potential applications in biotechnology and medicine, such as biosensors, drug delivery systems, and vaccine development. By using recombinant DNA technology, researchers can produce ModA proteins in larger quantities and with specific modifications, allowing for a better understanding of their functional mechanisms and ligand interactions. Moreover, the structural analysis of ModA can provide insights into the evolutionary adaptations of binding proteins in various organisms. The elucidation of ModA's structures and functions could pave the way for novel uses in synthetic biology and environmental bioremediation. Overall, the ongoing research into ModA recombinant proteins holds promise for advancing our knowledge of protein functionality and creating innovative solutions in multiple fields.
