Laminin Alpha 2 (LAMa2) is a large?sized alpha?chain subunit of laminin, a major structural glycoprotein residing in basement membranes across various tissues. It is predominantly expressed in skeletal muscle, peripheral nerves and placenta, assembling with other laminin subunits to form heterotrimeric laminin complexes that maintain basement?membrane integrity. This subunit mediates cell?matrix adhesion, stabilizes muscle cell membrane architecture, supports Schwann cell anchoring around nerve axons, and modulates cell proliferation, differentiation and tissue regeneration. Loss or mutation of LAMa2 frequently causes congenital muscular dystrophy and peripheral nerve dysmyelination, as impaired basement membrane assembly disrupts tissue mechanical support and intercellular signal transmission. Its expression level is finely tuned during development and tissue injury repair. LAMa2 associates with LAMC2 to constitute partial heterotrimeric laminin assemblies for basement membrane construction. To detect the activity of recombinant mouse LAMa2, a functional ELISA assay was performed to evaluate the interaction between recombinant mouse LAMa2 and recombinant human LAMC2. Briefly, biotin-linked LAMa2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100μl were then transferred to LAMC2-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37℃. Finally, add 50μl stop solution to the wells and read at 450nm immediately. The binding activity of mouse LAMa2 and human LAMC2 was shown in Figure 1, the EC50?for this effect is 0.135 μg/mL.