Analytical Data
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Gene name
tcyA
- Application
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Alternative Names
tcyA；yckK；L-cystine-binding Protein TcyA
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Species
Bacillus subtilis
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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
P42199
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Expression Region
20-268aa
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AA Sequence
CGAGNDNQSKDNAKDGDLWASIKKKGVLTVGTEGTYEPFTYHDKDTDKLTGYDVEVITEVAKRLGLKVDFKETQWDSMFAGLNSKRFDVVANQVGKTDREDKYDFSDKYTTSRAVVVTKKDNNDIKSEADVKGKTSAQSLTSNYNKLATNAGAKVEGVEGMAQALQMIQQGRVDMTYNDKLAVLNYLKTSGNKNVKIAFETGEPQSTYFTFRKGSGEVVDQVNKALKEMKEDGTLSKISKKWFGEDVSK
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Molecular Weight
29.6 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 tcyA gene, which encodes a component of the cysteine biosynthesis pathway, has garnered significant attention in recombinant protein research due to its critical role in cellular metabolism and stress response in various organisms. Cysteine is a key amino acid that serves as a building block for proteins, a precursor for important biomolecules, and plays a vital role in antioxidant defense mechanisms. Understanding the function and regulation of tcyA can provide insights into metabolic pathways and stress adaptations in microbes, plants, and potentially higher organisms. Research has shown that manipulating the expression of tcyA can enhance cysteine production, which is beneficial for biotechnological applications, including the production of nutraceuticals and pharmaceuticals. Furthermore, as cysteine can affect the synthesis of glutathione, a major antioxidant, studying tcyA may also illuminate strategies for improving stress tolerance in agricultural crops, aiding in food security. Advances in recombinant DNA technology have facilitated the cloning and expression of tcyA, allowing researchers to investigate its functional characteristics and interactions within cellular pathways. Overall, the study of tcyA as a recombinant protein presents an exciting avenue for both fundamental research and practical applications in biotechnology and agriculture.
