What is Laminin ?
Laminin has alive domains for collagen binding, corpuscle adhesion, heparin binding, and neurite bulge (PHD) fragment.1 Laminin chains are appointed A (molecular weight 400kDa), B1 (molecular weight 210 kDa) and B2 (molecular weight 200 kDa). The accord amid these chains is the aftereffect of abounding inter- and intrachain disulfide bonds. Together, they could cause the atom to attending like a crucifix.
Laminin is a above ECM protein basic of the basal lamina. In general, laminins are heterotrimeric glycoproteins with bounden regions for collagen, integrins, cellular domains, and proteoglycans such as dystroglycan. It aswell binds with itself to anatomy bedding in the basal lamina. Laminin is composed of a axial ~400 kDa alpha alternation with a capricious amount of annular regions and two ~200 kDa chains (beta and gamma) with circling α-helical and annular regions. Cysteine-rich repeats are accustomed in all the laminin chains.