Cat: IPD-X41387

Recombinant Bacillus thuringiensis cry1Bb Protein ,His & Myc

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Analytical Data

  • Gene name

    cry1Bb

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (140 kDa crystal protein)(Crystaline entomocidal protoxin)(Insecticidal delta-endotoxin CryIB(b))

  • Species

    Bacillus thuringiensis

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q45739

  • Expression Region

    1111-1229aa

  • Molecular Weight

    21.1 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

Cry1Bb recombinant protein is a crucial focus in agricultural biotechnology due to its potential to enhance crop resistance against certain pests, particularly lepidopteran insects. Derived from the bacterium *Bacillus thuringiensis* (Bt), Cry1Bb is one of several delta-endotoxins that exhibit insecticidal properties. The increasing reliance on chemical pesticides has prompted researchers to explore bio-based solutions that are more sustainable and environmentally friendly. Cry proteins, including Cry1Bb, function by binding to specific receptors in the gut of target insects, causing cell lysis and ultimately leading to pest death. Various studies have demonstrated its effectiveness when expressed in transgenic plants, significantly improving their resistance to pest infestations. Moreover, the use of Cry proteins aligns with integrated pest management strategies, reducing the need for chemical inputs while maintaining agricultural productivity. As pest resistance to traditional chemical insecticides becomes more common, the development and integration of Cry1Bb recombinant protein into crop systems is seen as a promising alternative. Ongoing research continues to explore the protein’s mechanisms, optimize its expression in plants, and assess its safety and ecological impact, paving the way for more resilient agricultural practices.

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