Laminin has been demonstrated to promote the attachment and growth of a variety of cells; used for the coating of culture dishes. It has been used for cell adhesion assay. It is recommended for use as a cell culture substratum at 1-2μg/cm2. The optimal concentration does depend on cell type as well as the application or research objectives.
Laminin from human fibroblasts has been used:
- in coating six-well plates for wound healing assay
- as a substrate in cell adhesion and spreading assay
- for differentiation of human embryonic stem cells (hESCs) and human induced pluripotent stem cells (hiPSCs) toward dopaminergic neurons
- in corneal endothelial cell wound healing (migration) assay and corneal endothelial cell barrier assay
Laminin from human fibroblasts is recommended for use as a cell culture substratum at 1-2 μg/cm
2. The optimal concentration does depend on cell type as well as the application or research objectives.
Laminin is purified as laminin-nidogen complex from mouse Engelbreth-Holm-Swarm (EHS) sarcoma. Laminin is a heterotrimer made from α, β and γ chain subunits. It is a glycoprotein which is required for the structural scaffolding of basement membranes. Laminin supports growth and differentiation of many cell types including epithelial, endothelial, neural, muscle and liver cells.
Biological activity: Tested for the promotion of adherence of HT-1080 cells.
Species specificity: Active on most mammalian cells.
Laminin proteins are integral components of structural scaffolding in animal tissues. They associate with type IV collagen via entactin and perlecan and bind to cell membranes through integrin receptors, dystroglycan glycoprotein complexes and Lutheran blood group glycoproteins. Laminin has active domains for collagen binding, cell adhesion, heparin binding, and neurite outgrowth fragment.
