Cat: IPD-X40152

Recombinant Phytophthora cryptogea cryptogein Protein ,His & Myc

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Analytical Data

  • Gene name

    cryptogein

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CRY

  • Species

    Phytophthora cryptogea

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P15570

  • Expression Region

    21-118aa

  • Molecular Weight

    17.3 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

Cryptogein is a class of proteins originally isolated from the plant pathogen *Cryptococcus neoformans*, which have garnered significant attention due to their unique structural properties and potential applications in biotechnology and medicine. Research into cryptogeins began with the recognition of their role in the pathogenicity of certain fungal species, where they assist in the modulation of host plant defenses. The study of cryptogeins has expanded to explore their molecular structures, which often feature intricate folding patterns and specific binding sites that have implications in both cell signaling and immune response modulation. Additionally, the ability to recombinant produce these proteins has opened avenues for further investigation into their functionality and therapeutic potential. Their unique characteristics place cryptogeins at the intersection of plant pathology, structural biology, and medical research, making them valuable subjects for elucidating mechanisms of disease resistance, developing novel bioactive compounds, and creating innovative biotechnological applications. As research advances, understanding the mechanisms by which cryptogeins interact with host systems could lead to breakthroughs in crop protection and the development of new strategies against fungal diseases.

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