Collagen Type IV, mouse

Type IV Collagen is a non-fibrillary network of different alpha-chains: alpha 1(IV) to-alpha 6(IV). It is typically found in basal membranes of different organs (e.g. skin, lens, lung, kidney). Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Murine collagen type IV 100%; murine collagen type I, II and III <0.1%; human collagen type IV and V <0.1%; murine fibronectin <0.1%; murine laminin <0.1% in RIA at 1:5000 dilution.