Recombinant Human GDF-15 (Human Cell-expressed) Protein Best Seller

Growth Differentiation Factor 15 (GDF-15), also called Macrophage Inhibitory Cytokine 1 (MIC-1), Placental Transforming Growth Factor beta, Prostate-derived Factor, and Placental Bone Morphogenetic Protein, is a divergent member of the Transforming Growth Factor beta (TGF-beta) superfamily (1, 2). Human GDF-15 shares 66% and 68% amino acid sequence identity with the rat and mouse proteins, respectively (3). GDF-15 is highly expressed in placenta and brain, and it is expressed at lower levels in kidney, pancreas, prostate, and colon. Similar to other TGF-beta family proteins, GDF-15 is synthesized as a large precursor protein that is cleaved at a dibasic cleavage site (RxxR) to release the mature protein. The C-terminal domain of GDF-15 contains seven characteristic conserved cysteine residues necessary for the formation of the cysteine knot and the single inter-chain disulfide bond (4, 5). Biologically active GDF-15 is a disulfide-linked homodimer of the mature protein. GDF-15 has been shown to have various functions, including inhibition of Tumor Necrosis Factor alpha (TNF-alpha) production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation (1, 6). GDF-15 also promotes neuronal survival, and hypothalamic expression of GDF-15 causes appetite suppression via modulation of neuropeptide Y and pro-opiomelanocortin levels (7-10). GDF-15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, promoting recovery following myocardial infarction, and regulating angiogenesis (11-15). Exposure of cardiomyocytes to GDF-15 results in Smad2 and Smad3 phosphorylation (16).