Analytical Data
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Gene name
cry1Fb
- Application
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Alternative Names
cry1Fb；cryIF(b)；cryINA67-1；Pesticidal crystal Protein Cry1Fb
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O66377
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Expression Region
984-1159aa
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AA Sequence
VKGHVDVEEQNNHRSVLVVPEWEAEVSQEVRVCPGRGYILRVTAYKEGYGEGCVTIHEVDNNTDELKFSSNCEKEQVYPGNTVACNDYNKNHGANACSSRNGGYDESYESNSSIPADYAPVYEEEAYTDGQRGNPCEFNRGHTPLPAGYVTAELEYFPETDTVWVEIGETEGTFIV
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Molecular Weight
22.8 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
Cry1Fb is a notable member of the Cry protein family, originally derived from the bacterium Bacillus thuringiensis (Bt). This family is well-known for its insecticidal properties and has been extensively studied for its potential applications in agricultural biotechnology. The research into Cry1Fb primarily focuses on its effectiveness against a range of agricultural pests, particularly lepidopteran insects, which pose significant threats to crop production. Understanding the structure and function of Cry1Fb, along with its mode of action at the molecular level, is crucial for developing genetically modified crops that express this protein, offering an environmentally friendly alternative to chemical pesticides. Recent studies have emphasized optimizing the expression of Cry1Fb in various host systems and exploring its efficacy in different environmental conditions. The ongoing research aims to enhance its insecticidal activity, broaden its target spectrum, and ensure its safety for non-target organisms, thereby advancing sustainable agricultural practices. Overall, the study of Cry1Fb recombinant protein plays a vital role in the quest for innovative solutions to improve crop resistance to pests and reduce the reliance on synthetic pesticides, contributing to food security and sustainable agriculture.
