Analytical Data
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Gene name
rpmE
- Application
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Alternative Names
rpmE; b3936; JW3907; 50S ribosomal protein L31; Large ribosomal subunit protein bL31-A
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Species
Escherichia coli
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A7M9
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Expression Region
1-70aa
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Molecular Weight
34.9 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 technology has revolutionized the field of molecular biology and biotechnology, allowing for the production of proteins that are otherwise difficult to obtain from natural sources. RPME (Recombinant Protein from E. coli) is a significant focus of research due to its potential applications in various domains, including therapeutics, diagnostics, and industrial processes. The rise of RPME is rooted in its advantages over traditional methods, such as higher yield, lower production costs, and the ability to perform post-translational modifications. As recombinant proteins can be engineered for specific functions, studies on RPME aim to optimize expression systems, purification methods, and functional characterization. Research has shown that RPME can be utilized in vaccine development, enzyme production, and as a research tool in understanding protein interactions and functions. The ability to express complex eukaryotic proteins in prokaryotic systems, such as E. coli, further enhances RPME's versatility. Consequently, ongoing studies continue to explore the molecular mechanisms underlying RPME expression and stability, with the ultimate goal of harnessing its full potential for innovative applications in medicine and industry.
