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Recombinant Human Filaggrin/FLG is a partial-length protein expressed with an N-terminal 6xHis-tag in the yeast. Its expression region corresponds to 3838-4061aa of human FLG protein. Its purity was determined by SDS-PAGE and reached up to 90%. This recombinant FLG protein may be used to synthesize antibodies against FLG or on the studies of FLG-associated signal transduction. FLG proteins in-stock are available. FLG is an epidermal differentiation protein that plays a fundamental role in the development and maintenance of the skin barrier. The binding of FLG with the intermediate keratin filaments leads to their aggregation and compaction, making cells collapse and flattening that is required for squame biogenesis. Within the squames, FLG undergoes further proteolysis and degrade into hygroscopic amino acids and other derivatives, which make up the natural moisturizing factor (NMF) responsible for water retention in the stratum corneum. FLG mutations perturb the skin barrier function, which causes ichthyosis vulgaris, increase the risk of atopic dermatitis and other atopic diseases.
Recombinant Human Filaggrin/FLG is a partial-length protein expressed with an N-terminal 6xHis-tag in the yeast. Its expression region corresponds to 3838-4061aa of human FLG protein. Its purity was determined by SDS-PAGE and reached up to 90%. This recombinant FLG protein may be used to synthesize antibodies against FLG or on the studies of FLG-associated signal transduction. FLG proteins in-stock are available.
FLG is an epidermal differentiation protein that plays a fundamental role in the development and maintenance of the skin barrier. The binding of FLG with the intermediate keratin filaments leads to their aggregation and compaction, making cells collapse and flattening that is required for squame biogenesis. Within the squames, FLG undergoes further proteolysis and degrade into hygroscopic amino acids and other derivatives, which make up the natural moisturizing factor (NMF) responsible for water retention in the stratum corneum. FLG mutations perturb the skin barrier function, which causes ichthyosis vulgaris, increase the risk of atopic dermatitis and other atopic diseases.
| Cat.No | ACP02584 | Target Name | FLG |
|---|---|---|---|
| Target Synonyms | ATOD2; Epidermal filaggrin; FILA_HUMAN; Filaggrin; Filaggrin precursor; Fillagrin; FLG; Profilaggrin | Form | Liquid or Lyophilized powder |
| Expression System | Yeast | Expression Range | 3838-4061aa |
| Mol Weight | 26.8kDa | Protein Length | Partial |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P20930 |
|---|
Uniprot Id
P20930
Target Species
Human
Target Name
FLG
Target Full Name
Filaggrin
Target Function
Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis.
Target Involvement
Ichthyosis vulgaris (VI); Dermatitis atopic 2 (ATOD2)
Target Subcellular Location
Cytoplasmic granule.
Target Protein Families
S100-fused protein family
Target Tissue Specificity
Expressed in skin, thymus, stomach, tonsils, testis, placenta, kidney, pancreas, mammary gland, bladder, thyroid, salivary gland and trachea, but not detected in heart, brain, liver, lung, bone marrow, small intestine, spleen, prostate, colon, or adrenal
Target Research Area
Signal Transduction, Cancer
Target Synonyms
ATOD2; Epidermal filaggrin; FILA_HUMAN; Filaggrin; Filaggrin precursor; Fillagrin; FLG; Profilaggrin
Target Background
The protein encoded by this gene is an intermediate filament-associated protein that aggregates keratin intermediate filaments in mammalian epidermis. It is initially synthesized as a polyprotein precursor, profilaggrin (consisting of multiple filaggrin units of 324 aa each), which is localized in keratohyalin granules, and is subsequently proteolytically processed into individual functional filaggrin molecules. Mutations in this gene are associated with ichthyosis vulgaris.
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