GDF15 (mouse):Fc (mouse) (rec.)

Chimerigen Laboratories

GDF15 (mouse):Fc (mouse) (rec.)

10

Research Use Only

>98%

Growth Differentiation Factor 15 (GDF15) is a divergent member of the TGF-beta superfamily. Cellular responses to TGF-beta proteins are mediated by hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. GDF15 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, GDF15 is synthesized as a large precursor protein that is cleaved at a dibasic cleavage site (RxxR) to release the mature protein. Mature mouse GDF15 shares 66% and 97% amino acid sequence identity with the human and rat proteins, respectively. The C-terminal domain of GDF15 contains seven characteristic conserved cysteine residues necessary for the formation of the cysteine knot and the single inter-chain disulfide bond. Biologically active GDF15 is a disulfide-linked homodimer of the mature protein. GDF15 has been shown to have various functions, including inhibition of TNF-alpha production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation. GDF15 promotes neuronal survival, and hypothalamic expression of GDF15 causes appetite suppression via modulation of neuropeptide Y and pro-opiomelanocortin levels. GFRAL and GDF15 signaling is implicated in diet-based obesity and insulin resistance. GDF15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, promoting recovery following myocardial infarction, and regulating angiogenesis. Exposure of cardiomyocytes to GDF15 results in Smad2 and Smad3 phosphorylation. - Recombinant protein. The extracellular domain of mouse GDF15 (aa 189-303) is fused to the N-terminus of the Fc region of mouse IgG2a. Measured by its binding ability in a functional ELISA. Source/Host: HEK 293 cells. Purity: >98% (SDS-PAGE). Lyophilized from 0.2microm-filtered solution in PBS. Growth Differentiation Factor 15 (GDF15) is a divergent member of the TGF-beta superfamily. Cellular responses to TGF-beta proteins are mediated by hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. GDF15 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, GDF15 is synthesized as a large precursor protein that is cleaved at a dibasic cleavage site (RxxR) to release the mature protein. Mature mouse GDF15 shares 66% and 97% amino acid sequence identity with the human and rat proteins, respectively. The C-terminal domain of GDF15 contains seven characteristic conserved cysteine residues necessary for the formation of the cysteine knot and the single inter-chain disulfide bond. Biologically active GDF15 is a disulfide-linked homodimer of the mature protein. GDF15 has been shown to have various functions, including inhibition of TNF-alpha production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation. GDF15 promotes neuronal survival, and hypothalamic expression of GDF15 causes appetite suppression via modulation of neuropeptide Y and pro-opiomelanocortin levels. GFRAL and GDF15 signaling is implicated in diet-based obesity and insulin resistance. GDF15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, promoting recovery following myocardial infarction, and regulating angiogenesis. Exposure of cardiomyocytes to GDF15 results in Smad2 and Smad3 phosphorylation.

2°C to 8°C,-20°C

12352202