CTGF Antibody

Connective Tissue Growth Factor (CTGF) is part of the CCN protein family, which includes six members in humans: Cyr61 (Cystein rich 61), CTGF, Nov (Nephroblastoma Overexpressed gene), and WISP-1, 2, and 3 (Wnt-1 Induced Secreted Proteins). These proteins are secreted and interact with the extracellular matrix (ECM) and cell membranes. CCN proteins, classified as matricellular proteins, regulate various cellular functions such as proliferation, differentiation, survival, adhesion, and migration. They are present in tissues derived from all three embryonic germ layers and contribute to the development of organs like the kidney, nervous system, muscle, bone marrow, cartilage, and bone. In adults, they play a role in wound healing, bone fracture repair, and pathological conditions like fibrosis, vascular diseases, and tumor development. Full-length CCN proteins can inhibit cell proliferation, while truncated versions may promote it and act as oncogenes. Structurally, the full-length protein has four modules. Module I shares similarities with Insulin-like Growth Factor Binding Proteins (IGFBPs). Module II contains a region resembling the Von Willebrand Factor Type C repeat (VWC). Module III includes a Thrombospondin type 1 repeat (TSP1)-like sequence, believed to be involved in cell adhesion and binding to sulfated glycoconjugates. Module IV, or the CT domain, encoded by exon 5, is essential for many CCN protein functions. While less conserved at the DNA level, it shows similarities to the CT domain of proteins like Von Willebrand's factor and mucins, and contains heparin-binding motifs. Proteolytic cleavage of secreted CCN2 and CCN3 can produce peptides with higher affinity for specific ligands compared to the full-length proteins. While truncated CCN2 isoforms exhibit biological activity, the same is not yet established for CCN3. The mechanism behind these truncated isoforms is unclear, but the cleavage occurs at the same amino acid position in both CCN2 and CCN3. Increased CCN2 expression has been observed in various conditions, including invasive mammary ductal carcinomas, dermatofibromas, pyogenic granulomas, endothelial cells of angiolipomas and angioleiomyomas, and pancreatic tumors. In chondrosarcomas, CCN2 expression correlates with tumor grade. CCN2's role in brain tumor angiogenesis is supported by its presence in both glioblastoma tumor cells and proliferating endothelial cells. In astrocytomas, higher CCN2 levels are linked to higher tumor grades, influencing cell proliferation. Inhibiting CCN2 leads to cell cycle arrest, while its overexpression promotes cell cycle progression. Around 50 genes potentially responsible for CCN2's proliferative effects have been identified. Furthermore, CCN2 is found in higher amounts in mononuclear cells of patients with acute lymphoblastic leukemia.

The solution contains 1mg/ml of the antibody in a buffer consisting of PBS at pH 7.4, 10% glycerol, and 0.02% sodium azide.

The CTGF antibody has been successfully tested for specificity and reactivity using ELISA, Western blot analysis, and ICC/IF. However, optimal working concentrations may vary depending on the specific application and should be determined experimentally.

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

CTGF antibody was purified by protein-A affinity chromatography.

PAT18E7AT.

Anti-human CTGF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTGF protein 27-349 amino acids purified from E. coli.

Mouse IgG_2a heavy chain and κ light chain.