FLG
FLG (filaggrin, also known as FLG1 or FLG-1) is an intermediate filament-associated protein that aggregates keratin filaments during terminal differentiation of mammalian epidermis. It is made as a large precursor, profilaggrin, and is linked to the skin disorder ichthyosis vulgaris. Browse Assay Genie's current range of FLG research reagents below, or read on for the biology behind the target.
FLG encodes filaggrin, a protein that aggregates keratin intermediate filaments and promotes disulfide-bond formation among those filaments during terminal differentiation of mammalian epidermis. Through this activity, filaggrin contributes to the organisation of keratin networks in the outermost, differentiating cells of the skin.
The FLG gene is not translated as a finished product. It is first synthesised as a polyprotein precursor, profilaggrin, which is built from multiple filaggrin units of 324 amino acids each and is localised in keratohyalin granules. Profilaggrin is then proteolytically processed into individual, functional filaggrin molecules. UniProt records the subcellular location of filaggrin as cytoplasmic granules, consistent with this granule-based storage of the precursor. This repeat-based architecture means that studies of the FLG gene and filaggrin protein often need to distinguish the precursor from its processed products.
Filaggrin belongs to the S100-fused protein family, and HGNC places FLG in the EF-hand domain containing group and the S100 fused type protein family. The symbol FLG1 and the alias FLG-1 appear in the literature alongside the approved name filaggrin. Mutations in the FLG gene are associated with ichthyosis vulgaris, which makes filaggrin a frequent subject in research on epidermal differentiation, keratin organisation and inherited skin conditions.
Filaggrin acts during terminal differentiation of mammalian epidermis, so it is a natural focus for studies of how keratinocytes mature.
Filaggrin aggregates keratin intermediate filaments and promotes disulfide-bond formation among them, making it relevant to cytoskeletal and structural studies.
Profilaggrin in keratohyalin granules is proteolytically cleaved into individual filaggrin molecules, a processing step that researchers examine in epidermal biology.
Mutations in the FLG gene are associated with ichthyosis vulgaris, supporting its use in research on inherited skin disorders.
FLG encodes filaggrin, which aggregates keratin intermediate filaments and promotes disulfide-bond formation among them during terminal differentiation of mammalian epidermis. It is made as the precursor profilaggrin, held in keratohyalin granules, and then proteolytically processed into individual filaggrin molecules.
The approved HGNC name is filaggrin, and the gene is also written FLG1 or FLG-1. The primary translation product is profilaggrin, a polyprotein of multiple 324-amino-acid filaggrin units, which is cleaved to release the individual functional filaggrin molecules.
Yes. According to the NCBI Gene summary, mutations in the FLG gene are associated with ichthyosis vulgaris. Filaggrin's role in organising keratin filaments in the epidermis is the context for this link. Check the datasheet of any product for its validated reactivity.
Other S100 fused type proteins, keratins and epidermal differentiation markers studied alongside filaggrin.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P20930; product specifications from Assay Genie datasheets.