Recombinant Mouse GDF-15 Protein, CF

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  • Purity
    >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured by its binding ability in a functional ELISA. When Recombinant Mouse GSF-15 is immobilized at 2 µg/mL (100 µL/well), the concentration of Recombinant Mouse Activin RIB/ALK-4 Fc Chimera (Catalog # 1477-AR) that produces 50% of the optimal binding response is approximately 1-6 μg/mL.
  • Source
    E. coli-derived mouse GDF-15 protein
    Ser189-Ala303
  • Accession #
  • N-terminal Sequence
    Analysis
    Ser189
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    13 kDa
  • SDS-PAGE
    9-13 kDa, reducing conditions
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8944-GD
 
Formulation Lyophilized from a 0.2 μm filtered solution in HCl.
 
Reconstitution Reconstitute at 250 μg/mL in 4 mM HCl.
 
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
 
Stability & Storage: 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.
 
Data Images
When Recombinant Mouse GDF-15 (Catalog # 8944-GD) is immobilized at 2 µg/mL (100 µL/well), the concentration of Recombinant Mouse Activin RIB/ALK-4 Fc Chimera (Catalog # 1477-AR) binds with a typical ED50 of 1-6 μg/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, respectively.
Background: GDF-15
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).
  • References:
    1. Unsicker, K. et al. (2013) Cytokine Growth Factor Rev. 24:373.
    2. Bootcov, M.R. et al. (1997) Proc. Natl. Acad. Sci. USA 94:11514.
    3. Fairlie, W.D. et al. (1999) J. Leukoc. Biol. 65:2.
    4. Fairlie, W.D. et al. (2001) J. Biol. Chem. 276:16911.
    5. Bauskin, A.R. et al. (2000) EMBO J. 19:2212.
    6. Paralkar, V.M. et al. (1998) J. Biol. Chem. 273:13760.
    7. Johnen, H. et al. (2007) Nat. Med. 13:1333.
    8. Strelau, J. et al. (2000) J. Neurosci. 20:8597.
    9. Breit, S.N. et al. (2011) Growth Factors 29:187.
    10. Strelau, J. et al. (2009) J. Neurosci. 29:13640.
    11. Whitson, R.J. et al. (2013) J. Cell. Biochem. 114:1424.
    12. Rossaint, J. et al. (2013) J. Thromb. Haemost. 11:335.
    13. Song, H. et al. (2012) Mol. Biol. Rep. 39:4017.
    14. Preusch, M.R. et al. (2013) Eur. J. Med. Res. 18:19.
    15. Kempf, T. et al. (2011) Nat. Med. 17:581.
    16. Xu, J. et al. (2006) Circ. Res. 98:342.
  • Long Name:
    Growth Differentiation Factor 15
  • Entrez Gene IDs:
    9518 (Human); 23886 (Mouse); 29455 (Rat)
  • Alternate Names:
    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
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Reconstitution Buffers
Description Application Cat# Citations Images  

Reconstitution Buffer 3 (HCl)

RB03
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