Recombinant Human LAYN protein

LAYNR (LAYilin), a transmembrane protein encoded by the *LAYN* gene, is a cell adhesion molecule initially identified for its role in regulating cytoskeletal dynamics and cell-matrix interactions. Structurally, it contains an extracellular hyaluronan-binding domain and a cytoplasmic tail that interacts with actin-binding proteins like talin and filamin. This architecture enables LAYN to act as a molecular bridge between extracellular matrix components and intracellular signaling pathways, modulating cell motility, adhesion, and mechanotransduction.

Originally discovered in fibroblasts, LAYN is highly expressed in immune cells, epithelial tissues, and certain cancers. Research highlights its dual role in physiological and pathological processes. In normal tissues, LAYN supports immune regulation by fine-tuning T-cell receptor signaling and maintaining immune tolerance. Conversely, in tumors, elevated LAYN expression correlates with immune evasion, metastatic potential, and poor prognosis. It suppresses anti-tumor immunity by upregulating immunosuppressive cytokines (e.g., IL-10) and recruiting regulatory T cells (Tregs) to the tumor microenvironment.

Recombinant LAYN proteins are engineered using mammalian or insect cell systems to preserve post-translational modifications and ligand-binding capacity. These proteins serve as critical tools for studying LAYN’s interactions with hyaluronan, integrins, and immune checkpoint pathways. Therapeutic applications focus on targeting LAYN to counteract immunosuppression in cancer or modulate autoimmune responses. Recent studies also explore its diagnostic potential as a biomarker for cancer progression and immunotherapy resistance. Despite functional overlaps with other adhesion molecules, LAYN’s unique signaling crosstalk and tissue-specific roles make it a compelling target for biomedical research.