Collagen Type II, bovine

Type II collagen is an alpha1(II)-trimer, which forms 67 nm cross-banded fibrils. Typically it can be observed in cartilage and various tumours. 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. Bovine collagen type II 100%, bovine collagen XI <3.0 %; bovine collagen I and IX <0.1% (RIA at 1:200 dilution).