Mouse GDF-8/Myostatin Propeptide Biotinylated Antibody
Mouse GDF-8/Myostatin Propeptide Biotinylated Antibody Summary
Asn25-Ser265
Accession # Q540E2
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Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: GDF-8/Myostatin
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.
- Guo, T. et al. (2009) PloS ONE 4:e4937.
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