Analytical Data
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Gene name
CHS1
- Application
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Alternative Names
Chitin-UDP acetyl-glucosaminyl transferase 1
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Species
Saccharomyces cerevisiae
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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
P08004
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Expression Region
4-200aa
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Molecular Weight
26.6 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
Related Products
Protein Description
CHS1, or Chitin Synthase 1, is a pivotal enzyme involved in the biosynthesis of chitin, a crucial component of fungal cell walls and exoskeletons in arthropods. In recent years, CHS1 has gained considerable attention due to its potential applications in biotechnology and medicine. Understanding the structure and function of CHS1 can reveal insights into fungal biology, offering promising targets for antifungal drug development, particularly in the face of increasing resistance to traditional antifungal agents. Moreover, CHS1 is essential for maintaining cell integrity, and its inhibition could lead to cell lysis in pathogenic fungi, thereby providing a novel strategy for controlling fungal infections. The recombinant production of CHS1 facilitates the study of its enzymatic properties, substrate specificity, and regulation, serving as a foundation for structure-function relationship analyses. Additionally, by utilizing recombinant techniques, researchers can produce significant quantities of purified CHS1 for high-throughput screening of potential inhibitors and explore its functional role in various organisms. Overall, research on CHS1 recombinant protein not only contributes to fundamental fungal biology but also holds the potential for new therapeutic approaches to combat fungal diseases.
