Analytical Data
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Gene name
Rubredoxin
- Application
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Alternative Names
Short name:Rd
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Species
Clostridium pasteurianum
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00268
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Expression Region
1-54aa
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Molecular Weight
22 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
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Protein Description
Rubredoxin is a small iron-sulfur protein that plays a crucial role in various biological processes, particularly in electron transfer and redox reactions within anaerobic microorganisms. This protein contains a single iron atom coordinated by four cysteine residues, facilitating the transfer of electrons in biochemical pathways such as those involved in respiration and fermentation. Research into recombinant rubredoxin has gained traction due to its potential applications in biotechnology and synthetic biology, including the development of bioelectronic devices and biosensors. The ability to produce rubredoxin recombinantly allows for the exploration of its structural and functional properties in greater detail, potentially leading to enhanced understanding of electron transfer mechanisms. Moreover, investigations into the enhancement of rubredoxin's stability and activity through engineering approaches presents opportunities for its utilization in industrial processes. Understanding how rubredoxin operates at a molecular level can also provide insights into similar proteins and lead to innovations in renewable energy solutions. Overall, the study of recombinant rubredoxin is significant not only for fundamental biochemistry but also for its applications in health, industry, and environmental sustainability.
