Analytical Data
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Gene name
ERG11
- Application
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Alternative Names
CYPLI Cytochrome P450 51 Cytochrome P450-14DM Cytochrome P450-LIA1 Sterol 14-alpha demethylase
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Species
Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10614
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Expression Region
1-20aa
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Molecular Weight
29.1 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
ERG11, also known as lanosterol 14α-demethylase, is a crucial enzyme in the ergosterol biosynthesis pathway, which is essential for the viability of various fungi, including pathogenic species such as Candida albicans and Aspergillus fumigatus. The enzyme catalyzes the demethylation of lanosterol, a precursor in the synthesis of ergosterol, which is a key component of fungal cell membranes. Due to its vital role in fungal biology, ERG11 represents an important target for antifungal drug development. Azole antifungals, such as fluconazole and itraconazole, inhibit ERG11, thereby disrupting ergosterol synthesis and compromising fungal cell membrane integrity. However, the emergence of azole-resistant fungal strains poses a significant challenge in clinical settings, making studies on ERG11 vital for understanding resistance mechanisms and developing new therapeutic strategies. Research on the recombinant expression of ERG11 can provide insights into its structure, function, and interaction with inhibitors, paving the way for the design of novel antifungals. Additionally, studying ERG11 can enhance our understanding of the evolutionary adaptations in fungal pathogens and assist in the identification of specific resistance mutations. Increasing knowledge about this enzyme is essential for overcoming current limitations in antifungal therapies and can lead to improved treatment options for invasive fungal infections, a growing concern in immunocompromised populations worldwide.
