Analytical Data
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Gene name
Cys
- Application
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Alternative Names
Cys；Cystin-1
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Species
Human
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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
P13500
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Expression Region
24-99aa
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AA Sequence
QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT
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Molecular Weight
13.7 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
Cysteine (Cys) recombinant proteins have garnered significant attention in recent years due to their essential role in various biological processes and their potential applications in biotechnology and medicine. Cysteine is a sulfur-containing amino acid that plays a critical role in protein structure and function, particularly through the formation of disulfide bonds, which contribute to the stability and activity of proteins. Research on Cys recombinant proteins focuses on optimizing their expression in various host systems, such as bacteria, yeast, and mammalian cells, to enhance yield and functionality. Advances in genetic engineering and protein expression technologies have facilitated the production of Cys-rich proteins, enabling scientists to explore their functions, interactions, and therapeutic potential. Additionally, the study of Cys in relation to redox biology and oxidative stress has opened new avenues for understanding diseases such as cancer and neurodegenerative disorders. As a result, Cys recombinant proteins are not only critical for fundamental research but also hold promise in developing novel therapeutic agents and diagnostic tools, making them a key focus of contemporary protein engineering efforts.
