LAYN Human

Layilin is characterized by its extracellular domain, which is involved in binding interactions, and a cytoplasmic domain that interacts with intracellular proteins . The extracellular domain of human Layilin (Met 1-Glu 220) is often expressed with a C-terminal fused Fc region of human IgG1 for recombinant protein production . This recombinant form is typically produced in HEK293 cells, a common host for protein expression .

Layilin plays a crucial role in cell adhesion and migration. It acts as a membrane-binding site for talin, an adaptor protein that mediates interactions between actin filaments and the cell membrane . The cytoplasmic domain of Layilin contains motifs that are sufficient for talin binding, facilitating the connection between the cytoskeleton and the cell membrane .

Additionally, Layilin is involved in the binding of hyaluronan, a glycosaminoglycan that is a major component of the extracellular matrix . This interaction is essential for various cellular processes, including cell motility and proliferation .

Recombinant human Layilin is produced using various expression systems, with the most common being mouse myeloma cell lines (NS0) and HEK293 cells . The recombinant protein is often purified to a high degree of purity (>95%) and is tested for endotoxin levels to ensure its suitability for research and therapeutic applications .

The recombinant form of Layilin is available in different formulations, including those with and without carrier proteins like Bovine Serum Albumin (BSA) . The presence of carrier proteins can enhance protein stability and shelf-life, making it suitable for various experimental applications .

Recombinant Layilin is used in various research areas, including cell biology, cancer research, and regenerative medicine . Its role in cell adhesion and migration makes it a valuable tool for studying cellular processes and developing therapeutic strategies.