Analytical Data
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Gene name
rnfH
- Application
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Alternative Names
rnfH；Protein RnfH
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Species
Coxiella
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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
B6IZH9
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Expression Region
1-101aa
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AA Sequence
MISIIIAYATPEKQVEIPLTVEESCTLVVAVKRSGILQQFPEINLSQAIVGIHNKRTALDAGLRDGDRIEIYRPLTMDPKQARLLRAKRGKIRRMVRGEAG
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Molecular Weight
27.3 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 rnfH gene, known to encode a Na+-translocating ferredoxin:NADP+ oxidoreductase, has garnered significant interest due to its role in energy metabolism in various microorganisms, particularly in anaerobic environments. This enzyme is crucial for the biological conversion of energy from electron donors to applicable forms for cellular processes. The study of recombinant rnfH proteins has grown in relevance as researchers seek to elucidate the mechanistic details of Na+ transport and its coupling to redox reactions, which are fundamental to bioenergetics. Investigating rnfH recombinants can provide insights into the evolution of electron transport systems, highlight potential biotechnological applications, and improve our understanding of microbial physiology under different environmental conditions. Furthermore, characterizing the recombinant protein's structure and function can pave the way for innovative approaches in metabolic engineering, bioenergy production, and bioremediation strategies, contributing to sustainable development. Overall, the exploration of rnfH and its recombinant variants stands at the intersection of microbiology, biochemistry, and applied sciences, making it a vital area of study.
