Analytical Data
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Gene name
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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Alternative Names
Ribulose-Phosphate 3-Epimerase; RPE; HUSSY-17
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96AT9-1
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Expression Region
M1-R228
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Protein Length
Full Length of Isoform-1
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Molecular Weight
26.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
