Analytical Data
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Gene name
bLg
- Application
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Alternative Names
bLg；hnsB；DNA-binding Protein StpA
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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
Q29614
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Expression Region
1-174aa
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AA Sequence
MKFLLLTVGLALIGAIQAVENIRSKNDLGVEKFVGSWYLREAAKTMEFSIPLFDMDIKEVNLTPEGNLELVLLEKADRCVEKKLLLKKTQKPTEFEIYISSESASYTFSVMETDYDSYFLFCLYNISDREKMACAHYVRRIEENKGMNEFKKILRTLAMPYTVIEVRTRDMCHV
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Molecular Weight
20.2 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
The study of bLg (bovine lactoglobulin) recombinant protein has gained significant attention due to its crucial roles in the dairy industry and potential health benefits. As a major whey protein in bovine milk, bLg is known for its high nutritional value, functional properties, and ability to enhance the texture and stability of dairy products. However, its natural extraction from milk poses challenges such as variability in yield and purity. Consequently, researchers have turned to recombinant DNA technology to produce bLg in microorganisms like bacteria, yeast, and fungi, enabling more consistent and scalable production. This approach not only improves the availability of bLg for various applications, including food formulations, nutraceuticals, and pharmaceuticals, but also provides insights into its structural and functional characteristics. The recombinant expression of bLg allows for the exploration of its immunological properties, potential allergenic effects, and the ability to modify its amino acid composition for targeted applications. Understanding the molecular mechanisms and interactions of bLg in food systems aids in the development of innovative products that meet consumer demands for health and sustainability. Overall, the research surrounding bLg recombinant protein stands at the intersection of food science, biotechnology, and nutrition, with promising implications for enhancing dairy product quality and addressing global health challenges.
