Analytical Data
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Gene name
Lb
- Application
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Alternative Names
/
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Species
Pisum sativum
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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
Q9SAZ1
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Expression Region
2-146aa
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Molecular Weight
19.9 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 research background of Lb (Lactobacillus bulgaricus) recombinant proteins is rooted in the increasing interest in probiotics and their applications in food and health industries. Lactobacillus bulgaricus is a well-known lactic acid bacterium used in the production of yogurt and other fermented dairy products, and it has shown potential health benefits, including immune modulation and gut health improvement. With advances in biotechnology, researchers have begun to explore the possibility of expressing recombinant proteins using Lb as a host, which could enhance the functional properties of these proteins. The ability to produce specific proteins through genetic engineering opens up new avenues for developing functional foods and therapeutic agents. Studies have shown that Lb can efficiently express heterologous proteins, making it an attractive system for the production of enzymes, peptides, and other bioactive compounds. This research not only aims at improving the nutritional value of food products but also addresses the need for sustainable and cost-effective methodologies for protein production. Moreover, as the global demand for probiotics and functional foods continues to rise, utilizing Lb for recombinant protein production holds promise for the advancement of health-oriented innovations, potentially leading to new therapies for various health conditions while enhancing food safety and quality. Consequently, this area of research has garnered significant attention in both academia and industry, highlighting the importance of Lb as a versatile platform for biotechnology applications.
