Analytical Data
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Gene name
CSBF
- Application
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Alternative Names
AP-57; C10orf99; Chromosome 10 Open Reading Frame 99; Antimicrobial peptide-57
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6UWK7
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Expression Region
Met1~Val81
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Molecular Weight
30kDa
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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 study of CSBF (Cysteinyl-Sulfinate Betaine Fermentation) recombinant proteins has gained significant attention in recent years due to their potential applications in biotechnology and medicine. CSBF is derived from a unique metabolic pathway that enables certain microorganisms to convert cysteine into valuable bioactive compounds, contributing to various physiological processes and health benefits. Researchers are particularly interested in the recombinant production of CSBF proteins to enhance their availability and functionality. By utilizing techniques such as genetic engineering and synthetic biology, scientists aim to optimize the expression of these proteins in suitable host organisms. This research not only contributes to a deeper understanding of cysteine metabolism but also explores the therapeutic potential of CSBF proteins in treating conditions related to oxidative stress and inflammation. Furthermore, the ability to produce these proteins in a recombinant manner opens up avenues for large-scale production, making them more accessible for pharmaceutical applications. Overall, the investigation into CSBF recombinant proteins represents a promising frontier in the quest for innovative solutions in health and nutrition.
