Analytical Data
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Gene name
cry2Ab
- Application
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Alternative Names
71KDA crystal protein;Crystaline entomocidal protoxinInsecticidal delta-endotoxin CryIIA(b)
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Species
Bacillus thuringiensis subsp. kurstaki
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21254
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Expression Region
1-633aa
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Molecular Weight
74.7 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
Cry2Ab is a bioactive protein derived from the bacterium Bacillus thuringiensis (Bt), known for its insecticidal properties, particularly against lepidopteran pests. The research on Cry2Ab protein primarily focuses on its potential applications in agriculture, specifically in the development of genetically modified (GM) crops that exhibit enhanced resistance to insect herbivores. This resistance is critical for sustainable agriculture, as it can significantly reduce reliance on chemical pesticides, thereby minimizing environmental impact and increasing crop yields. Additionally, studies have shown that Cry2Ab can be effective against various pest species, which makes it a promising candidate for further investigation in biopesticide formulations. Understanding the molecular mechanisms through which Cry2Ab exerts its insecticidal action is essential for optimizing its usage and enhancing its effectiveness in pest management strategies. Research efforts also include investigating the safety profile of Cry2Ab to ensure it does not adversely affect non-target organisms and human health. As a result, the study of Cry2Ab recombinant protein is a vital area of research in the fields of entomology, molecular biology, and agricultural biotechnology, aiming to develop innovative solutions for pest control while promoting ecological balance and food security.
