Decorin from bovine articular cartilage

Decorin from bovine articular cartilage is a proteoglycan that belongs to the small leucine-rich repeat proteoglycans and proteins (SLRPs) family. Decorin is present in almost all tissues. It has a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions.

Decoran is a small proteoglycan composed of a chondroitin/dermatan sulfate glycosaminoglycans attached to a 40 kDa core protein. It is found primarily in the extracellular matrix of articular cartilage. Decorin interacts with collagen types I and II via its core protein wherein it delays fibrillogenesis. Decorin also interacts with fibronectin, thrombospondin and TGF-β isoforms, and the EGF-receptor.

Decorin from bovine articular cartilage has been used in solid phase binding assay (ELISA), binding assays, binding inhibition assay, parasite binding assays, scaffold fabrication, quartz crystal microbalance assay, inhibition of CSA (chondroitin sulphate A) binding assay and glycans and glycan biotinylation.

Decorin plays an important role in guiding the proper assembly of collagen during fibrillogenesis. Deficiency in decorin results in altered tissue structure and function. It controls growth factors like EGF and TGF-β. Decorin blocks aggregation of fibrils into fibers and fibrillogenesis in cell-free constructs of polymerized type I collagen.

Decorin is an approx. 100 kDa proteoglycan consisting of a 40 kDa core protein and one chondroitin or dermatan sulfate glycosaminoglycan chain. From 0.2 μm filtered solution prior to lyophilization.