Analytical Data
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Gene name
rpmG
- Application
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Alternative Names
rpmG；C2orf1；Large ribosomal subunit Protein bL33m
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Species
E.coli
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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
P0A7N9
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Expression Region
2-54aa
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AA Sequence
AKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKI
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Molecular Weight
33.1 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
The research on the RPMG recombinant protein is situated within the broader context of understanding the biological roles and potential applications of recombinant proteins in various fields, including medicine, biotechnology, and enzymology. RPMG, or Rhizobium etli Phosphate-Mobilizing Glycerol, is a protein associated with phosphate solubilization, a critical process for nutrient availability in agricultural ecosystems. As soil phosphates are often in forms inaccessible to plants, microorganisms like Rhizobium play a pivotal role in mineralizing these compounds, thereby enhancing soil fertility and plant growth. The study of RPMG aims to elucidate its structure-function relationship and underlying mechanisms that facilitate phosphate mobilization. By generating recombinant RPMG, researchers can investigate its biochemical properties, interaction with other macromolecules, and functional pathways in detail. Furthermore, there is increased interest in utilizing such proteins for biotechnological applications, such as biofertilizers and biocontrol agents in sustainable agriculture. Understanding RPMG's function not only contributes to fundamental microbiological knowledge but also offers insights into environmentally friendly practices to enhance crop productivity, thus addressing global food security challenges. As the world grapples with soil degradation and declining agricultural yields, the exploration of recombinant proteins like RPMG holds promise for innovative solutions that align with the principles of sustainable development.
