Analytical Data
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Gene name
OmcA
- Application
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Alternative Names
OmcA；envA；Small cysteine-rich outer membrane Protein omcA
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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
P0CZ19
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Expression Region
20-87aa
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AA Sequence
CCRIVDCCFEDPCAPKPCNPCGNKKDKGCSPCGVYTPSCSKPCGSECNPGVQGPQAKGCTSLDGRCKQ
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Molecular Weight
14.6 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
The study of the recombinant protein OmcA is rooted in its significant role in the extracellular electron transfer processes of certain microorganisms, particularly Geobacter species, which are known for their ability to transfer electrons to solid electron acceptors such as metal oxides. As a crucial component of microbial fuel cells and bioremediation strategies, OmcA facilitates energy conversion and pollutant degradation, making it a target of interest for bioenergy and environmental applications. Understanding its structure, function, and the mechanisms underlying its electron transfer capabilities can provide insights into optimizing microbial processes for renewable energy generation. Recent advancements in recombinant DNA technology have enabled researchers to produce OmcA in heterologous systems, allowing for extensive biochemical and biophysical characterization. This research not only aims to elucidate the electrochemical properties of OmcA but also seeks to engineer variants with enhanced functionality, thereby improving the efficiency of bioelectrochemical systems. The integration of OmcA into synthetic biology platforms holds the potential to revolutionize energy production and bioremediation approaches, paving the way for environmentally sustainable technologies.
