Analytical Data
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Gene name
ERG26
- Application
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Species
SVG-Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53199
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Expression Region
1-349aa
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Molecular Weight
46.1 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
ERG26 reconstituted protein is a crucial component in the study of ergosterol biosynthesis, particularly in yeasts and fungi. Ergosterol, a sterol found in fungal cell membranes, is analogous to cholesterol in animal cells and plays a vital role in maintaining membrane integrity and fluidity. The ERG26 gene encodes a key enzyme in the ergosterol biosynthetic pathway, specifically responsible for the conversion of 24-methylated sterols into ergosterol. Understanding the function and regulation of ERG26 is essential, as disruptions in this pathway can lead to impaired cellular growth and increased susceptibility to antifungal treatments, such as azoles. Furthermore, studying the ERG26 protein can provide insights into resistance mechanisms that some fungi develop against commonly used antifungal agents. Characterizing the properties and interactions of the ERG26 protein through recombinant expression systems has significant implications for both fundamental biology and the development of novel therapeutic strategies. Investigating this protein enhances our understanding of fungal physiology and could lead to improved antifungal drug design, addressing the growing challenge of antifungal resistance in clinical settings. Thus, research on ERG26 not only contributes to the basic understanding of fungal biology but also holds potential for practical applications in medicine and agriculture.
