Analytical Data
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Gene name
cla
- Application
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Alternative Names
/
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Species
Aspergillus clavatus
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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
P0CL71
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Expression Region
28-177aa
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Molecular Weight
24.5 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 on CLA (Conjugated Linoleic Acid) recombinant proteins has garnered significant interest due to their potential health benefits and applications in food science and biotechnology. CLA is a group of fatty acids found in certain meat and dairy products, known for its anti-cancer, anti-obesity, and immunomodulatory properties. However, obtaining CLA in sufficient quantities from natural sources can be challenging. Thus, the development of recombinant proteins that can efficiently synthesize or modulate CLA production has emerged as a promising strategy. By leveraging genetic engineering techniques, researchers aim to create microbial or plant-based systems capable of producing these beneficial fatty acids. This approach not only offers an alternative to traditional extraction methods but also paves the way for sustainable production processes. Furthermore, studying CLA recombinant proteins provides insights into their mechanisms of action at the molecular level, facilitating the identification of optimal conditions for enhanced production. As the demand for functional foods and nutraceuticals continues to rise, the exploration of CLA recombinant proteins holds the potential to revolutionize dietary supplementation and improve human health outcomes. Ultimately, this research contributes to the broader understanding of fatty acid biology and opens avenues for innovative applications in nutrition and medicine.
