Analytical Data
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基因名
loiP
- Application
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别名
yggG
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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
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P25894
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表达区间
19-252aa
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分子量
29 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
LoiP, short for "Lysine Oligomer-Induced Protein," is a novel recombinant protein that has garnered attention in the field of biotechnology and molecular biology due to its unique structural and functional properties. The study of LoiP arises from the increasing demand for proteins with specific functionalities, such as enhanced stability, improved solubility, and bioactivity, which are crucial for applications in therapeutic development, industrial processes, and research. Recombinant DNA technology has facilitated the production of LoiP by allowing the integration of specific genetic sequences into host organisms, resulting in proteins that can be engineered to possess desirable traits. The exploration of LoiP is also motivated by its potential applications in drug delivery systems, enzyme engineering, and as a scaffold for vaccine development. Moreover, understanding the mechanisms behind LoiP's stability and interaction with other biomolecules can provide insights into protein folding and aggregation, key factors that influence the efficacy of therapeutic proteins. As researchers continue to investigate LoiP's properties and applications, it represents a promising avenue for the development of innovative solutions to various challenges in science and medicine.
