Analytical Data
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Gene name
cysP
- Application
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Alternative Names
cysP; b2425; JW2418; Thiosulfate-binding protein
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Species
Escherichia coli
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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
P16700
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Expression Region
26-338aa
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Molecular Weight
48.0 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
The cysP gene encodes a key enzyme involved in the biosynthesis of cysteine, an essential amino acid crucial for various biological functions, including protein synthesis, antioxidant defense, and cellular signaling. Research into cysP recombinant protein has gained attention due to its potential applications in biotechnology and medicine. Cysteine is not only vital for the structure and function of proteins but also acts as a precursor for glutathione, a critical antioxidant in the body. By producing cysP in a recombinant form, scientists can study its enzymatic properties, mechanisms of action, and regulatory pathways in detail, which may lead to advancements in metabolic engineering, synthetic biology, and therapeutic interventions for diseases related to cysteine metabolism. Furthermore, understanding the functional aspects of cysP can facilitate the development of novel strategies for enhancing cysteine production in microbial systems, thereby addressing nutritional deficiencies and improving industrial processes in the food and pharmaceutical sectors. The ability to manipulate cysP expression and activity presents exciting possibilities for both fundamental research and practical applications, making it a significant target for ongoing investigations in biochemical and molecular biology.
