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Recombinant Mouse GDF-8 Propeptide Fc Chimera Protein

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity

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Catalog# & Formulation Size Price
Carrier Free
6986-PG-025/CF
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Recombinant Mouse GDF-8 Propeptide Fc Chimera Protein Summary

Details of Functionality
Measured by its ability to inhibit rmGDF-8 activity in K562 human chronic myelogenous leukemia cells. Thies, R.S. et al. (2001) Growth Factors 18:251. The ED50 for this effect is 0.03-0.15 μg/mL in the presence of 40 ng/mL of Recombinant Mouse GDF‑8/Myostatin.
Source
Mouse myeloma cell line, NS0-derived mouse GDF-8/Myostatin protein
Mouse GDF-8 Propeptide
(Asn25-Arg267) with a substitution Ser265Arg
Accession # NP_034964		 IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asn25
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Mstn
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
54.9 kDa (monomer).
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
66 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES, NaCl and CHAPS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse GDF-8 Propeptide Fc Chimera Protein

  • GDF8
  • GDF-8
  • GDF8growth differentiation factor 8
  • growth/differentiation factor 8
  • MSLHP
  • MSTN
  • Myostatin

Background

Growth Differentiation Factor 8 (GDF‑8), also known as Myostatin, is a secreted TGF‑ beta superfamily protein that is expressed specifically in developing and adult skeletal muscle. It controls myoblast proliferation and is a potent negative regulator of skeletal muscle mass (1‑3). Mouse GDF‑8 is synthesized as a 376 amino acid (aa) preproprotein that consists of a 24 aa signal peptide, a 243 aa propeptide, and a 109 aa mature protein (2). Within the propeptide, mouse GDF‑8 shares 96% and 99% aa sequence identity with human and rat GDF‑8, respectively. GDF‑8 is secreted as a preproprotein that is cleaved by BMP‑1 family proteases to separate the 35‑40 kDa propeptide from the 12 kDa bioactive mature protein (4‑6). This results in a latent complex containing a disulfide‑linked dimer of the mature protein and two noncovalently‑associated molecules of the propeptide (2, 6). The GDF‑8 propeptide functions as an inhibitor of mature GDF‑8, and GDF‑8 activity can also be inhibited through association with Follistatin, FLRG, Decorin, or GASP‑1 (6‑11). The uncleaved GDF‑8 proprotein binds Latent TGF‑ beta  binding protein 3 (LTBP3) which can sequester it in the extracellular matrix and prevent the proteolytic cleavage of the propeptide (12). GDF‑8 binds to the type II Activin receptor Activin RIIB which then associates with the type I receptors Activin RIB/ALK‑4 or TGF‑ beta  RI/ALK‑5 to induce signaling (13). GDF‑8 additionally inhibits adipogenic differentiation of human bone marrow‑derived mesenchymal stem cells and preadipocytes (14). Genetic deletion of GDF‑8 or in vivo administration of the GDF‑8 propeptide induces muscle hypertrophy as well as enhanced glucose utilization and insulin sensitivity and a reduction in overall fat mass (15, 16).
  1. McPherron, A.C. (2010) Immunol. Endocr. Metab. Agents Med. Chem. 10:217.
  2. McPherron, A.C. et al. (1997) Nature 387:83.
  3. Zimmers, T.A. et al. (2002) Science 296:1486.
  4. Wolfman, N.M. et al. (2003) Proc. Natl. Acad. Sci. 100:15842.
  5. McFarlane, C. et al. (2005) Dev. Biol. 283:58.
  6. Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. 98:9306.
  7. Thies, R.S. et al. (2001) Growth Factors 18:251.
  8. Amthor, H. et al. (2004) Dev. Biol. 270:19.
  9. Hill, J.J. et al. (2002) J. Biol. Chem. 277:40735.
  10. Miura, T. et al. (2006) Biochem. Biophys. Res. Commun. 340:675.
  11. Hill, J.J. et al. (2003) Mol. Endocrinol. 17:1144.
  12. Anderson, S.B. et al. (2008) J. Biol. Chem. 283:7027.
  13. Rebbapragada, A. et al. (2003) Mol. Cell. Biol. 23:7230.
  14. Guo, W. et al. (2008) J. Biol. Chem. 283:9136.
  15. Matsakas, A. et al. (2009) Neuromuscul. Disord. 19:489.
  16. Guo, T. et al. (2009) PloS ONE 4:e4937.

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Bioinformatics

Gene Symbol Mstn
Uniprot