Analytical Data
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Gene name
FLG
- Application
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Alternative Names
Profilaggrin
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20930
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Expression Region
Arg3049~Ala3361
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Molecular Weight
59kDa
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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
FLG (filaggrin) is a crucial protein involved in skin barrier function, playing a significant role in the formation of the stratum corneum, the outermost layer of the skin. Its main biological function is to aggregate keratin fibers, which contributes to the structural integrity and hydration of the skin. Aberrations in FLG expression have been associated with various skin conditions, including atopic dermatitis, ichthyosis vulgaris, and other skin disorders characterized by compromised barrier function. The study of FLG recombinant proteins has gained attention as a potential therapeutic avenue for restoring skin barrier integrity and treating skin diseases. Researchers are focusing on FLG's structure, function, and interactions with other skin proteins to develop recombinant forms that retain the native protein’s activity. These recombinant proteins can be utilized in skin treatments, helping to improve hydration, reduce transepidermal water loss, and mitigate inflammation. The ongoing research aims to understand the precise mechanisms by which FLG contributes to skin health, which could lead to innovative solutions for skin barrier repair and the treatment of related dermatological conditions. The insights gained from FLG recombinant protein studies are expected to enhance our understanding of skin biology and provide valuable therapeutic options for patients suffering from skin barrier-related issues.
