Analytical Data
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Gene name
RPE
- Application
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Alternative Names
RPE;Ribulose-phosphate 3-epimerase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-228aa
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AA Sequence
MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFG HPVVESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAGANQYTFHLEATEN PGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAI MRSEDPRSVINLLRNVCSEAAQKRSLDRVDHHHHHH
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Molecular Weight
26 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 become a pivotal technique in molecular biology and biotechnology, driven by the need for proteins for research, therapeutic, and industrial applications. The background of RPE stems from the limitations of traditional protein extraction methods, which often yield insufficient quantities of proteins from natural sources and may introduce contaminants. The advent of genetic engineering techniques in the 1970s facilitated the isolation of specific genes and their subsequent insertion into expression systems, such as bacteria, yeast, and mammalian cells. As a result, researchers have been able to produce large amounts of proteins with high purity and consistency, enhancing the understanding of protein function and structure. This methodology has significantly contributed to the development of biologics, including monoclonal antibodies and vaccines, addressing critical health challenges. Additionally, RPE has applications in agriculture, where designer proteins can be produced for pest resistance and improved crop yield. Overall, the evolution of recombinant protein technology represents a crucial intersection of biology and engineering, enabling groundbreaking discoveries and innovations across various fields.
