Cat: IPD-X29203

Recombinant Human Cry2 Protein (Baculovirus),His & Myc

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Analytical Data

  • Gene name

    Cry2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    KIAA0658

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q49AN0

  • Expression Region

    1-593aa

  • Molecular Weight

    70.8

  • 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

Cry2 recombinants are a class of proteins derived from the Cry family of insecticidal proteins produced by the bacterium Bacillus thuringiensis (Bt). These proteins are well-known for their biological pest control capabilities, particularly in agricultural settings, where they provide an environmentally friendly alternative to chemical pesticides. The Cry proteins function by binding to specific receptors in the gut cells of target insects, leading to cell lysis and ultimately insect death. Research into Cry2 has gained particular interest due to its effectiveness against a broad spectrum of agricultural pests, including lepidopteran larvae. Genetic modifications and recombinant DNA technology have enabled scientists to produce Cry2 proteins in various systems, enhancing their stability and efficacy while reducing non-target effects. Studies on the structure-function relationships of Cry2 have unveiled insights into its mechanism of action, receptor interactions, and the potential for creating engineered variants with improved insecticidal properties. Additionally, advancements in biotechnology have opened avenues for integrating Cry2 into transgenic crops, which can express these proteins directly, thus providing sustained pest resistance and reducing the need for external pesticide applications. The exploration of Cry2's efficacy, specificity, and potential environmental impacts continues to be a significant area of research, contributing to sustainable agricultural practices and food security. As the demand for sustainable pest management solutions rises, the development of Cry2-based technologies holds promise for addressing the challenges posed by insect resistance to conventional pesticides and the necessity for sustainable agricultural development.

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