Analytical Data
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Gene name
CLOST_2292
- Application
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Alternative Names
CLOST_2292Ferredoxin
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Species
Acetoanaerobium sticklandii
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P80168
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Expression Region
2-56aa
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Molecular Weight
13.0 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
CLOST_2292 is a gene found in the bacterium Clostridium acetobutylicum, a well-studied organism for its biofuel production capabilities. This gene encodes a protein with a proposed role in carbohydrate metabolism, which could be crucial for understanding the organism's fermentation processes. The study of CLOST_2292 is significant due to its potential applications in industrial biotechnology, particularly in optimizing fermentative pathways for the production of solvent-based biofuels and chemicals. Furthermore, Clostridium species are key players in anaerobic digestion and bioremediation, making the investigation of their metabolic enzymes essential for advancing bioprocess technologies. By characterizing the CLOST_2292 recombinant protein, researchers aim to elucidate its structural and functional properties, contributing to the broader understanding of microbial metabolism in energy production. Understanding the role of this protein could lead to enhanced metabolic engineering strategies to improve yield and efficiency in biofuel production, addressing global energy challenges and supporting the development of sustainable bioprocesses.
