||Lactadherin is a widely distributed glycoprotein (~ 50 kDa), which was originally characterized due to its association with milk fat/lipid globule membranes. Synonymous names are PAS-6/7, bovine-associated mucoprotein, BA-46, P47, and MFG-E8. Structural hallmarks of lactadherin are the presence of two epidermal growth factor (EGF) homology domains (with an RGD peptide motif in the second EGF domain), and two C domains sharing homology with the discoidin family of lectin domains including the phospholipid-binding domains of blood clotting factors V and VIII. Lactadherin shows preferential binding to phosphatidylserine (L-form) in a calcium independent manner.
||Milk, also secreted by stimulated macrophages, vascular smooth muscle, endothelial cells
||TBS, 1% BSA, 0.02% azide, pH 7.4
||52 kDa and 47 kDa
||>95% by SDS-PAGE. NOT tissue/cell culture grade. Not tested for endotoxin.
||Extinction coefficient:16.5, Plasma concentration: unknown in normal adults, measurable in women with metastatic breast cancer, measurable in newborn calves after milk meal, Percent carbohydrate: 6%, 13% for glycosylation variants, Structure:single chain with two EGF domains and two C domains. The mouse isoform contains a central proline rich region and the human molecule contains a single EGF domain