Analytical Data
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Gene name
Oleosin
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简介
Oleosins are essential for stabilizing liposomes during seed drying, preventing oil coalescence and underscoring their importance in seed physiology. It binds to lipid and phospholipid moieties, suggesting a multifunctional molecular interaction that contributes to liposome integrity. Oleosin Protein, Glycine max (Cell-Free, His) is the recombinant Oleosin protein, expressed by E. coli Cell-free , with N-10*His labeled tag.
- Application
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Alternative Names
Oleosin
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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
C6SZ13
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Expression Region
M1-S147
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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 proteins are a crucial component of plant oil bodies, which are essential for seed oil storage and metabolism. These proteins function as a barrier, stabilizing oil droplets and preventing them from coalescing, thereby contributing to the efficiency of oil storage in seeds. The study of oleosins has gained significant attention due to their potential applications in biotechnology and food science. Understanding the structure and function of oleosins can lead to advancements in the genetic engineering of oilseeds to enhance oil yield and quality. Additionally, oleosins play a role in plant responses to environmental stress, making them important for improving crop resilience. Recombinant oleosin proteins can be produced in various expression systems for further functional analysis and characterization, paving the way for innovative uses in the production of biofuels, edible oils, and bioplastics. Research into oleosin recombination involves exploring the native functionality of these proteins, understanding their interactions with lipids and other cellular components, and optimizing their expression conditions for industrial applications. This area of study not only contributes to our fundamental knowledge of plant biology but also has significant implications for agriculture and sustainability in the face of global food demands.
