Analytical Data
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基因名
iolG
- Application
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别名
Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase ;MI 2-dehydrogenase/DCI 3-dehydrogenase
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种属
Bacillus subtilis
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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
P26935
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表达区间
1-344aa
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分子量
54.4 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 iolG recombinant protein is significant in the field of microbial biochemistry and genetics, particularly concerning the metabolism of inositol. IolG, a key enzyme in the inositol catabolic pathway, is responsible for the conversion of inositol to myo-inositol-1-phosphate, playing a crucial role in the utilization of inositol as a carbon source in various microorganisms. Understanding the structure and function of the iolG gene product can provide insights into microbial adaptation to different nutritional environments and can facilitate biotechnological applications such as biofuel production and bioremediation. The recombinant expression of iolG allows for the detailed study of the enzyme's kinetics, mechanism, and regulation, which is essential for engineering microbial strains with enhanced metabolic capabilities. Furthermore, exploring the evolutionary variations of iolG across different species can yield information about metabolic diversity and the evolutionary pressures that shape microbial lifestyles. Consequently, research on iolG recombinant protein not only enhances our comprehension of fundamental biochemical processes but also opens avenues for innovative applications in industrial biotechnology.
