Connective tissue growth factor (UniProt P29279; also known as CCN family member 2, Hypertrophic chondrocyte-specific protein 24, IBP-8, IGF-binding protein 8, IGFBP-8, Insulin-like growth factor-binding protein 8) is encoded by the CTGF (also known as CCN2, HCS24, IGFBP8) gene (Gene ID 1490) in human. CTFG is one the three founding members of the CCN (Ctgf, Cyr61, and Nov) family of proteins involved in a wide array of cellular activities, including migration, proliferation, extracellular matrix synthesis, adhesion, survival, differentiation, and apoptosis. CTGF acts an autocrine mediator of transforming growth factor-beta (TGF-beta) in fibroblasts. CCN proteins are characterized by a more than 10% cysteine content and an absolute conservation of the position of their 38 cysteine residues. Human CTGF is synthesized with a signal peptide sequence (a.a. 1-26), the removal of which yields the mature protein with an N-terminal IGF-binding protein (IGFBP) domain (a.a. 27-98), followed by a von Willebrand factor type C (VWC or VWFC) domain (a.a. 101-167), a cysteine-free hinge region (a.a. 168-197), thrombospondin type-1 (TSP-1) domain (a.a. 198-243), and a C-terminal cysteine-knot or C-terminal CYS-KNOT (CTCK) motif (a.a. 256-330). Due to the high number of disulfide bridges, most of the CTGF domains are resistant to proteolytic digestion, and most proteases primarily cleave only in the cysteine-free hinge region, producing almost exclusively intact N- and C-terminal half fragments. The N-terminal half of CTGF is shown to mediate differentiation and collagen synthesis in concert with IGF-2, while its C-terminal half mediates cell proliferation in concert with EGF.
Synonyms: Connective tissue growth factor, CCN family member 2, Hypertrophic chondrocyte-specific protein 24, IBP-8, IGF-binding protein 8, IGFBP-8, Insulin-like growth factor-binding protein 8
Application: Western Blotting Analysis: A representative lot detected the N-terminal (1-180), but not C-terminal (181-349), fragment derived from baculovirus expressed human CTGF by chymotrypsin cleavage. The N-terminal fragment appeared as a doublet due to differential glycosylation (Grotendorst, G.R., and Duncan, M.R. (2005). FASEB J. 19(7):729-738).Neutralizing Analysis: A representative lot inhibited CTGF-stimulated collagen synthesis, but not CTGF-stimulated DNA synthesis, in rat kidney (NRK) fibroblasts (Grotendorst, G.R., and Duncan, M.R. (2005). FASEB J. 19(7):729-738).Note: It is recommended that gel electrophoresis be performed under non-reducing condition to effectively separate CTGF N- and C-terminal fragments, as well as differentially glycosylated N-terminal fragments.
Other Notes: Concentration: Please refer to lot specific datasheet.