Analytical Data
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Gene name
FLG
- Application
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Alternative Names
FLG;Filaggrin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
3838-4061aa
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AA Sequence
DSSRHSQSGQGESAGSRRSRRQGSSVSQDSDSEAYPEDSERRSESASRNHHGSSREQSRDGSRHPGSSHRDTASHVQSSPVQSDSSTAKEHGHFSSLSQDSAYHSGIQSRGSPHSSSSYHYQSEGTERQKGQSGLVWRHGSYGSADYDYGESGFRHSQHGSVSYNSNPVVFKERSDICKASAFGKDHPRYYATYINKDPGLCGHSSDISKQLGFSQSQRYYYYE
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Molecular Weight
39.4 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 study of FLG (filaggrin) recombinant proteins has gained significant attention due to their critical role in skin barrier function and the pathogenesis of various dermatological conditions. Filaggrin is a key protein in the epidermis, involved in the aggregation of keratin filaments, which contributes to the structural integrity of the skin. Deficiencies or mutations in the FLG gene have been linked to atopic dermatitis, ichthyosis vulgaris, and other skin disorders, highlighting the protein's importance in maintaining skin hydration and barrier properties. Researchers are increasingly focusing on recombinant FLG proteins as a potential therapeutic approach to restore skin barrier function and alleviate symptoms in affected individuals. By employing techniques such as recombinant DNA technology and protein engineering, scientists aim to produce functional FLG proteins that can be used in skin care products or as treatments for skin conditions. This research not only aims to enhance our understanding of skin biology but also to develop innovative therapeutic strategies to improve the quality of life for individuals suffering from skin-related diseases. Overall, the exploration of FLG recombinant proteins holds promise for advancing dermatological therapies and expanding our knowledge of the interplay between genetics and skin health.











