Application

Western Blotting Analysis: A representative lot detected the C-terminal (181-349), but not N-terminal (1-180), fragment derived from baculovirus expressed human CTGF by chymotrypsin cleavage (Grotendorst, G.R., and Duncan, M.R. (2005). FASEB J. 19(7):729-738).
Neutralizing Analysis: A representative lot inhibited CTGF-stimulated DNA synthesis, but not CTGF-stimulated collagen 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.

This Anti-CTGF Antibody, C-Term is validated for use in Western Blotting, Neutralizing for the detection of CTGF.

General description

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.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Purified goat polyclonal antibody in 0.3 M Glycine, 50 mM Tris, pH 8.0 without preservatives.

Quality

Evaluated by Western Blotting of chymotrypsin-cleaved CTGF fragments.

Western Blotting Analysis: 1.0 µg/mL of this antibody detected 1 ng of the C-terminal (181-349), but not N-terminal (1-180), fragment derived from baculovirus expressed human CTGF by chymotrypsin cleavage.

Specificity

This polyclonal antibody was affinity-purified using the purified C-terminal fragment (181-349) from chymotrypsin-cleaved rhCTGF to eliminate immunoreactivity against the N-terminal half (1-180) of CTGF in the original goat antiserum raised against full-length rhCTGF (Grotendorst, G.R., and Duncan, M.R. (2005). FASEB J. 19(7):729-738).

Target description

35.92/38.09 kDa (isoform Long mature/pro-form), 19.14 kDa (isoform Long C-terminal fragment; a.a. 181-349), 33.04/35.21 kDa (isoform Short mature/pro-form) calculated.