Analytical Data
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Gene name
Trypsin inhibitor DE-3
- Application
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Alternative Names
Trypsin inhibitor DE-3
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Species
Others
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Source
P. pastoris
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09943
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Expression Region
V1-S172
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Protein Length
Full Length
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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
Trypsin inhibitor DE-3, derived from the seeds of the common bean (Phaseolus vulgaris), is a crucial protein that specifically inhibits the activity of trypsin, an important digestive enzyme in various organisms. The study of this recombinant protein has garnered significant interest due to its potential applications in agriculture, food science, and medicine. By understanding the mechanisms of trypsin inhibition, researchers aim to improve protein digestion in livestock, enhance the nutritional value of animal feed, and develop novel therapeutic agents for treating diseases related to protease dysfunction. Furthermore, the recombinant expression of Trypsin inhibitor DE-3 allows for the production of large quantities of this protein for experimental purposes, facilitating investigations into its structure-function relationships and interactions with other biological molecules. The exploration of its properties can lead to innovative strategies for pest control in crops, as well as the enhancement of the functional properties of food products. Overall, research on Trypsin inhibitor DE-3 not only contributes to the fundamental understanding of plant defense mechanisms but also promises valuable applications across various biotechnological fields.
