In a functional ELISA, Recombinant Mouse GDF-15 (Catalog # 8944-GD) binds to Recombinant Mouse GFR alpha -like Fc Chimera (9844-GR) with an ED50 of 0.500-5.00 ng/mL.
1 μg/lane of Recombinant Mouse GDF-15 (Catalog # 8944-GD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 10.5 kDa and 22 kDa, ...read more
Measured by its binding ability in a functional ELISA. Recombinant
Mouse GDF-15 (Catalog # 8944-GD) binds to Recombinant Mouse GFR alpha -like
Fc Chimera (Catalog #
9844-GR)
with an ED50 of 0.500-5.00 ng/mL.
Source
E. coli-derived mouse GDF-15 protein Ser189-Ala303
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
13 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
9-13 kDa, reducing conditions
Publications
Read Publications using 8944-GD in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in 4 mM HCl.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse GDF-15 Protein, CF
GDF15
GDF-15
growth differentiation factor 15
growth/differentiation factor 15
Macrophage inhibitory cytokine 1
MIC-1
MIC-1NSAID-activated gene 1 protein
MIC1Prostate differentiation factor
NAG-1
NAG-1NSAID-regulated gene 1 protein
NSAID (nonsteroidal inflammatory drug)-activated protein 1
PDF
PDFGDF-15
PLAB
PLABNRG-1
Placental bone morphogenetic protein
Placental TGF-beta
PTGF-beta
PTGFBPTGF-beta
Background
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. Cellular responses to TGF-beta proteins are mediated by hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors (1-3). 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. Mature mouse GDF-15 shares 66% and 97% amino acid sequence identity with the human and rat proteins, respectively. 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 TNF-alpha production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation (2, 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).
Unsicker, K. et al. (2013) Cytokine Growth Factor Rev. 24:373.
Bootcov, M.R. et al. (1997) Proc. Natl. Acad. Sci. USA 94:11514.
Fairlie, W.D. et al. (1999) J. Leukoc. Biol. 65:2.
Fairlie, W.D. et al. (2001) J. Biol. Chem. 276:16911.
Bauskin, A.R. et al. (2000) EMBO J. 19:2212.
Paralkar, V.M. et al. (1998) J. Biol. Chem. 273:13760.
Johnen, H. et al. (2007) Nat. Med. 13:1333.
Strelau, J. et al. (2000) J. Neurosci. 20:8597.
Breit, S.N. et al. (2011) Growth Factors 29:187.
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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