Analytical Data
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Gene name
Canavalin
- Application
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Species
Canavalia gladiata
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10562
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Expression Region
27-445aa
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Molecular Weight
55.0 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
Canavalin is a seed storage protein derived from the jack bean (Canavalia ensiformis) known for its potential nutritional and therapeutic applications. Research into Canavalin has gained attention due to its rich amino acid profile, particularly its content of essential amino acids, making it a valuable source of plant-based protein. Several studies have focused on the recombinant expression of Canavalin to enhance its yield and biological functionality, allowing for better performance in various applications, such as food, pharmaceuticals, and biotechnological fields. Through genetic engineering techniques, researchers aim to produce Canavalin with improved stability, solubility, and bioactivity, which could lead to its incorporation into functional foods or nutraceuticals. Furthermore, understanding the structure-function relationship of Canavalin can provide insights into protein interactions and its role in the immune response. The ongoing exploration of Canavalin at the molecular level underscores its significance as both a model protein for biotechnological studies and a promising candidate for addressing nutritional needs globally.
