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 (His) is the recombinant human-derived RPE protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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Alternative Names
Ribulose-Phosphate 3-Epimerase; Ribulose-5-Phosphate-3-Epimerase; RPE; HUSSY-17
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Species
Human
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Source
E. coli
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Tag
C-6*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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AA Sequence
MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLDR
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Protein Length
Full Length of Isoform-1
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Molecular Weight
26-28 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
Related Products
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.
