Laminins are heterotrimeric glycoproteins and are major components of the basement membrane. Each laminin is comprised of a single alpha, beta, and gamma chain that heterotrimerize via their coiled-coil domains to form a large cruciform-shaped molecule. Mature Laminin  alpha 4 is a subunit of Laminin 411, Laminin 421, and Laminin 423. Mature Laminin alpha 4 is a 1792 amino acid (aa) residue protein that has a Laminin N-terminal domain, four Laminin EGF-like domains, the coiled-coil domain, and five C‑terminal tandem Laminin G-like domains. The G-like domains contain binding sites for integrin, heparin, and dystroglycan. Within the region used as immunogen, mouse Laminin  alpha 4 shows 91% and 97% aa sequence identity with human and rat Laminin  alpha 4, respectively.