Decorin from bovine articular cartilage

General description
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 is a proteoglycan that belongs to the small leucine-rich repeat proteoglycans and proteins (SLRPs) family. Decorin is present in almost all tissues.[1] It has a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions.[2] Application
Decorin from bovine articular cartilage has been used in solid phase binding assay (ELISA)[3], binding assays[4], binding inhibition assay[5], parasite binding assays[6], scaffold fabrication[7], quartz crystal microbalance assay[8], inhibition of CSA (chondroitin sulphate A) binding assay[9] and glycans and glycan biotinylation.[10] Biochem/physiol Actions
Decorin plays an important role in guiding the proper assembly of collagen during fibrillogenesis.[1] 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.[1] Other Notes
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.