Human Laminin  alpha 4 Antibody

Laminin alpha 4 (LAMA-4 [Laminin subunit alpha 4]; also Laminin-14/423, -8/411 and -9/421 subunit alpha) is a 180-230 kDa secreted member of the laminin family of molecules. It is found in the basement membranes of adipocytes, endothelial cells, cardiac and visceral smooth muscle cells, fibroblasts, keratinocytes, and pancreatic acinar cells. Laminin is a heterotrimeric glycoprotein that attaches cells to basement membranes. It is composed of covalently-linked alpha -, beta - and gamma -chains, and is known to attach cells to basement membranes. In the case of the alpha -subunit, this is mediated through binding to multiple integrins ( alpha 3 beta 1, alpha v beta 3 and alpha 6 beta 1), plus dystroglycan and the syndecans-2 and -4. Mature human Laminin alpha 4 is 1799 amino acids (aa) in length (aa 25-1823). It contains multiple domains, including four EGF‑like domains (aa 82-255) and five Laminin G-like domains (aa 833-1820). There is a chondroitin sulfate attachment at the N‑terminus that accounts for 20-30 kDa of MW. Laminin alpha 4 is cleaved between the Laminin G-like 3 and 4 domains, creating a soluble 44 kDa fragment that possesses antibacterial activity. There are two potential splice variants, one that shows a deletion of aa 266-272, and another that contains a 55 aa substitution for aa 66-1823. Over aa 826-1816, human Laminin alpha 4 shares 91% aa sequence identity with mouse Laminin alpha 4.