Cat: PA2000-1960

Recombinant Human ERG11 Protein,His

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Analytical Data

  • Gene name

    ERG11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ERG11;cyp51;Lanosterol 14-alpha demethylase erg11

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10614

  • Expression Region

    1-20aa

  • AA Sequence

    MSATKSIVGEALEYVNIGLS

  • Molecular Weight

    29.1 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

ERG11, also known as cytochrome P450 51 (CYP51), is a key enzyme involved in the biosynthesis of ergosterol, a crucial component of fungal cell membranes. This protein has gained significant attention in the field of medical mycology and pharmacology, primarily due to its role in conferring resistance to antifungal agents, particularly azoles, which inhibit ergosterol synthesis. The emergence of azole-resistant fungal strains has become a pressing public health concern, necessitating a deeper understanding of ERG11's structure, function, and mutation patterns. Research into the recombinant expression of ERG11 allows for the detailed study of its enzymatic activity and interaction with antifungal drugs. By producing ERG11 in a controlled laboratory setting, researchers can investigate how specific mutations in the ERG11 gene contribute to resistance mechanisms, aiding the development of new therapeutic strategies. Furthermore, characterizing the biochemical pathways regulated by ERG11 can help identify potential drug targets. Overall, the study of ERG11 at a molecular level is critical for advancing our understanding of fungal pathogenesis and developing effective treatments against resistant strains.

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