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 0.05-0.25 µg/mL in the presence of 5 ng/mL of Recombinant Mouse GDF‑8/Myostatin. Approximately 1 µg/mL will completely inhibit GDF-8 activity in these cells.
Source
Mouse myeloma cell line, NS0-derived mouse GDF-8/Myostatin protein Asn25-Ser265, with a C-terminal 10-His tag
>90%, 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
28.7 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
39 kDa, reducing conditions
Publications
Read Publications using 1539-PG/CF 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 PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
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 Protein, CF
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 bp3 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 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).
McPherron, A.C. (2010) Immunol. Endocr. Metab. Agents Med. Chem. 10:217.
McPherron, A.C. et al. (1997) Nature 387:83.
Zimmers, T.A. et al. (2002) Science 296:1486.
Wolfman, N.M. et al. (2003) Proc. Natl. Acad. Sci. 100:15842.
McFarlane, C. et al. (2005) Dev. Biol. 283:58.
Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. 98:9306.
Thies, R.S. et al. (2001) Growth Factors 18:251.
Amthor, H. et al. (2004) Dev. Biol. 270:19.
Hill, J.J. et al. (2002) J. Biol. Chem. 277:40735.
Miura, T. et al. (2006) Biochem. Biophys. Res. Commun. 340:675.
Hill, J.J. et al. (2003) Molecular Endocrinology 17:1144.
Anderson, S.B. et al. (2008) J. Biol. Chem. 283:7027.
Rebbapragada, A. et al. (2003) Mol. Cell. Biol. 23:7230.
Guo, W. et al. (2008) J. Biol. Chem. 283:9136.
Matsakas, A. et al. (2009) Neuromuscul. Disord. 19:489.
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