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Description
Collagens consist in 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 cosists in a tripel-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. Type II collagen is an alpha1(II)-trimer, MW 95 kDa, which forms 67 nm cross-banded fibrils. Typically it can be observed in skin, cartilage and various tumours.
Immunogen
A purified preparation of lathyritic type II collagen from embryonic chicken sternum. Remarks: Epitope: Carboxyl-terminal one quarter of the type II collagen. The epitope for2B1. 5 MAb is not susceptible to digestion of lathyritic type II collagen with recombinantstromelysin.