Analytical Data
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Gene name
Oleosin L
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简介
The oleosin L protein plays a structural role in stabilizing liposomes during seed drying, preventing oil coalescence and affecting liposome integrity. Its potential interactions with lipid and phospholipid moieties suggest the involvement of multiple molecules. Oleosin L Protein, Sesamum indicum (Cell-Free, His) is the recombinant Oleosin L protein, expressed by E. coli Cell-free , with N-10*His labeled tag.
- Application
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Alternative Names
Oleosin L; Allergen Ses i 5; Oleosin 15 kDa
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Species
Others
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Source
E. coli Cell-free
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Tag
N-10*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9XHP2
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Expression Region
M1-S145
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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
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Protein Description
Oleosin L is a member of the oleosin protein family, which plays a crucial role in plant seed oil bodies, acting as a stabilizing component that prevents coalescence and maintains the integrity of oil droplets. The study of Oleosin L has gained significant attention due to its potential applications in biotechnology, particularly in the field of oil production and food science. Researchers aim to understand the structure-function relationship of Oleosin L to enhance oil stability and improve the nutritional quality of seed oils. Additionally, the ability to genetically manipulate and express Oleosin L in various systems, including yeast and plants, opens up avenues for producing bioengineered oils with desirable properties. The exploration of Oleosin L also contributes to the broader understanding of lipid metabolism and storage in plants, which is vital for enhancing crop yields and developing sustainable agricultural practices. This interest is further fueled by the increasing global demand for vegetable oils and the necessity to optimize oil production in an environmentally friendly manner. As a result, studies focused on the recombinant expression of Oleosin L not only provide insights into its functional mechanisms but also pave the way for innovative applications in bioengineering, nutrition, and sustainable food resources.
