>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human GDF-15 is used at 0.5 µg/mL, the concentration of
Recombinant Human Activin RIB/ALK-4 Fc Chimera (Catalog #
that produces 50% of the optimal binding response is approximately 0.5-3 μg/mL.
When Recombinant Human GDF-15 (Catalog # 9279-GD) is used at 0.5 µg/mL, Recombinant Human Activin RIB/ALK-4 Fc Chimera (Catalog # 808-AR) binds with an ED50 of 0.5-3 μg/mL.
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 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, the GDF-15 proprotein is cleaved at a dibasic cleavage site (RxxR) to release the mature protein (4). The C-terminal domain of GDF-15 contains seven characteristic conserved cysteine residues necessary for the formation of the cysteine knot and the single interchain disulfide bond (5). Biologically active GDF-15 is a disulfide-linked homodimer of the mature protein and signals through the heterodimeric receptor composed of TGF-beta RI/ALK-5 and TGF-beta RII (6). GDF-15 has been shown to have various functions, including inhibition of TNF-alpha production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation (1, 5). GDF-15 also promotes neuronal survival, and hypothalamic expression of GDF-15 causes appetite suppression via modulation of Neuropeptide Y and Pro-opiomelanocortin levels (7-9). GDF-15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, inhibiting CXCL1-induced neutrophil adhesion, regulating angiogenesis, and inhibiting norepinephrine-induced mycardial hypertrophy (6, 10-15).
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Unsicker, K. et al. (2013) Cytokine Growth Factor Rev. 24:373.
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Fairlie, W.D. et al. (2001) J. Biol. Chem. 276:16911.
Paralkar, V.M. et al. (1998) J. Biol. Chem. 273:13760.
Artz, A. et al. (2016) Blood 128:529.
Johnen, H. et al. (2007) Nat. Med. 13:1333.
Strelau, J. et al. (2000) J. Neurosci. 20:8597.
Strelau, J. et al. (2009) J. Neurosci. 29:13640.
Whitson, R.J. et al. (2013) J. Cell. Biochem. 114:1424.
Rossaint, J. et al. (2013) J. Thromb. Haemost. 11:335.
Song, H. et al. (2012) Mol. Biol. Rep. 39:4017.
Preusch, M.R. et al. (2013) Eur. J. Med. Res. 18:19.
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