CTGF is a member of the CCN family of secreted cysteine-rich regulatory proteins, and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial and epithelial cells, and binds to IGF, TGF-beta1 and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans. CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Mature Human CTGF is a 38.0 kDa secreted protein containing 323 amino acid residues. CTGF is comprised of four distinct structural domains (modules), which are identified as IGF-Binding Protein (IGF-BP), von Willebrand Factor C (VWFC), Thrombospondin type I (TSP type I), and C-terminal cysteine knot-like (CTCK) domains. Full length CTGF can be proteolytically cleaved in certain tissues to yield N-terminal truncated isoforms, which, depending on the isoform, contain only the TSP type I and CTCK domains or contain only the CTCK domain. Recombinant Human CTGF is an 11.0 kDa protein consisting of 97 amino acid residues.