Anti Decorin (Bone Proteoglycan II) mAb (Clone 889C7)

Decorin is a ubiquitous small ECM proteoglycan that is closely related in structure to, biglycan, and which belongs to the small leucine-rich proteoglycan (SLRP) subfamily. Its core protein may be found frequently associated with the cell surface and normally carries a single chondroitin sulfate or dermatan sulfate chain. Its molecular mass in fully glycosylated/glycanated form varies from 90-240 kDa, while its unglycosylated/unglycanated core protein has a Mr of about 45 kDa. Decorin interacts with several ECM components, including fibrillar collagens, fibronectin, thrombospondin and C1q and plays a role in collagen fibrillogenesis. Decorin is upregulated in cancer, inflammed and degenerating tissues, and is critically involved in wound-healing. Infusion of decorin into experimental rodent spinal cord injuries has been shown to suppress scar formation and promote axon growth. Decorin affects various types of cancer by down-regulating the activity of several receptors involved in cell growth and survival. Decorin binds to and modulates the signaling of the epidermal growth factor receptor and other members of the ErbB family of receptor tyrosine kinases. It exerts its antitumor activity by a dual mechanism: via inhibition of these key receptors through their physical downregulation coupled with attenuation of their signaling, and by binding to and sequestering TGF-beta. Decorin also modulates the insulin-like growth factor receptor and the low-density lipoprotein receptor-related protein-1, which indirectly affects the TGF-beta receptor pathway. Gene deletion of decorin causes skin defects, manifested as irregularly shaped collagen type III fibrils of the dermis. Mutations in the decorin gene cause congenital stromal corneal dystrophy.