Analytical Data
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Gene name
CutA
- Application
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Alternative Names
Cutin hydrolase
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Species
Colletotrichum capsici
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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
P10951
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Expression Region
17-228aa
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Molecular Weight
35.0 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
Related Products
Protein Description
CutA proteins are a family of membrane-associated proteins that play crucial roles in the homeostasis of metals, particularly copper, in various organisms. They are of significant interest due to their potential implications in understanding metal transport and detoxification mechanisms, especially in the context of environmental stress and cellular health. Many studies highlight the importance of CutA proteins in microbial resistance to metal toxicity, making them valuable targets for biotechnological applications, including bioremediation and bioengineering. The recombinant expression of CutA proteins allows researchers to investigate their structure, function, and interaction with metal ions in controlled conditions. By elucidating the mechanisms underlying CutA activity, scientists aim to develop strategies to combat metal-induced toxicity, improve metal recovery processes, and enhance the efficacy of biotechnological systems. Recent advances in recombinant DNA technology have facilitated the production of these proteins in various expression systems, providing a platform for biochemical and biophysical studies. This research not only contributes to our fundamental understanding of metal biology but also paves the way for innovative applications in environmental and industrial biotechnology.
