Analytical Data
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基因名
RPE
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简介
The RPE Protein is responsible for catalyzing the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. RPE Protein, Human (HEK293, His) is the recombinant human-derived RPE protein, expressed by HEK293 , with C-His labeled tag.
- Application
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别名
Ribulose-Phosphate 3-Epimerase; RPE; HUSSY-17
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种属
Human
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表达系统
HEK293
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标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96AT9-1
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表达区间
M1-R228
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蛋白长度
Full Length of Isoform-1
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分子量
26.4 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
Recombinant protein _expression (RPE) has emerged as a pivotal technique in biotechnology and molecular biology, enabling the production of proteins that are essential for various applications in research, medicine, and industry. The development of RPE systems began in the late 20th century, driven by the increasing demand for proteins with specific characteristics, such as enzymes, antibodies, and hormones. Traditional methods of protein extraction from natural sources often proved inadequate due to low yields and the complexity of purification processes. The advent of recombinant DNA technology allowed for the manipulation of genetic material, facilitating the cloning of desired protein coding sequences into expression vectors. These vectors can be introduced into host organisms, such as bacteria, yeast, or mammalian cells, which then produce the target proteins in higher quantities. This method not only enhances the efficiency of protein production but also allows for modifications that can improve stability, activity, and specificity. RPE is instrumental in various fields, including therapeutic drug development, vaccine production, and the creation of diagnostic tools. As research continues to advance, optimizing expression systems and improving post-translational modifications remain critical areas of exploration, ensuring that RPE continues to evolve to meet the growing needs of scientific and medical advancements.
