Analytical Data
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基因名
iceE
- Application
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别名
Ice nucleation protein
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种属
Enterobacter agglomerans
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表达系统
Yeast
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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
P16239
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表达区间
1129-1258aa
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分子量
15.7 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
The study of iceE recombinant protein originates from the need to understand and manipulate the mechanisms of protein expression in extreme environments. IceE, a gene derived from psychrophilic organisms, has been shown to play a crucial role in cold adaptation, allowing these microorganisms to thrive at low temperatures. Researchers are particularly interested in the iceE gene due to its potential applications in biotechnology and industrial processes, where cold-active enzymes can enhance efficiency and reduce energy costs. The expression and characterization of IceE recombinant protein provide insights into its structural and functional properties, which can be leveraged for the development of innovative biocatalysts. Additionally, understanding the evolutionary adaptations that enable psychrophiles to function in frigid conditions offers valuable information that can inspire advances in enzyme engineering and cold-process biomanufacturing. The research contributes to a broader understanding of protein adaptations to environmental extremes, which is relevant not only to biotechnology but also to ecological and evolutionary studies.
