Analytical Data
-
Gene name
rnfH
- Application
-
Alternative Names
rnfH; CbuG_0706; Protein RnfH
-
Species
Coxiella burnetii
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B6IZH9
-
Expression Region
1-101aa
-
Molecular Weight
27.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 encodes a key protein in the respiratory chain of certain anaerobic bacteria, particularly within the "Reducer of Nitrate and Iron" (Rnf) complex, which plays a critical role in energy metabolism. Research into rnfH recombinant protein has gained traction due to its potential applications in bioenergy production, bioremediation, and understanding microbial electron transfer mechanisms. The Rnf complex is known to facilitate electron transfer from reduced substrates to ferredoxin, thereby contributing to ATP synthesis in an ATPase-independent manner, which is a vital process for microbes thriving in low-energy environments. Investigating the structure and function of the rnfH protein, therefore, promises to enhance our knowledge of microbial ecology, metabolic pathways, and the development of innovative biotechnological solutions. Recent studies utilizing recombinant DNA technology have enabled the expression and purification of rnfH in heterologous systems, allowing researchers to explore its biochemical properties in detail. This research not only aids in deciphering the complex roles of rnfH in bacterial energy conservation but also provides a platform for potential applications in the development of bio-based energy solutions, offering a sustainable approach to addressing global energy demands. Furthermore, understanding the dynamics of rnfH and its associated pathways could illuminate broader aspects of microbial physiology and adaptability, emphasizing its significance in both fundamental and applied microbiology. Overall, the recombinant protein research on rnfH is poised to contribute significantly to our understanding of anaerobic respiration and its implications for environmental and industrial applications.
