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 (His) is the recombinant human-derived RPE protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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别名
Ribulose-Phosphate 3-Epimerase; Ribulose-5-Phosphate-3-Epimerase; RPE; HUSSY-17
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种属
Human
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表达系统
E. coli
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标签
C-6*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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氨基酸序列
MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLDR
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蛋白长度
Full Length of Isoform-1
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分子量
26-28 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 molecular biology and biotechnology, facilitating the production of proteins that are crucial for various applications, including drug development, vaccine production, and basic research. Traditional methods of protein extraction from natural sources often yield insufficient quantities and can be fraught with impurities. RPE addresses these challenges by utilizing genetically engineered organisms, such as bacteria, yeast, or mammalian cells, to produce target proteins in a controlled environment. This method allows for the optimization of protein yield, activity, and post-translational modifications, ensuring that the recombinant proteins exhibit functionalities similar to their naturally occurring counterparts. Furthermore, RPE has gained significant attention due to its role in creating biologics, including monoclonal antibodies and therapeutics, that are essential in treating myriad diseases, from cancers to autoimmune disorders. As the demand for high-quality proteins continues to grow, advancements in RPE, including improved expression systems and purification techniques, are crucial for accelerating research and enhancing the development of new biopharmaceuticals. Thus, ongoing research in this field is vital for addressing both scientific inquiries and clinical needs in modern medicine.
