Recombinant Human/Mouse/Rat GDF-8/Myostatin Protein, CF

Recombinant Human/Mouse/Rat GDF-8/Myostatin Protein (Catalog # 11658-G8) induces cytotoxicity on MCP-11 cells. The ED50 for this effect is 4.00-40.0 ng/mL.

1 μg/lane of Recombinant Human/Mouse/Rat GDF‑8/Myostatin Protein (Catalog # 11658-G8) was resolved with SDS-PAGE under reducing (R) condition and visualized by silver staining, showing bands at 10-14 kDa.

• Reactivity: Hu, Mu, Rt
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human/Mouse/Rat GDF-8/Myostatin Protein, CF Summary

• Details of Functionality: Measured by its ability to induce cytotoxicity using MPC-11 mouse B lymphocyte cells. The ED₅₀ for this effect is 4.00-40.0 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived GDF-8/Myostatin protein
  Asp267-Ser375
• Accession #: O14793.1
• N-terminal Sequence: Asp267
• Structure / Form: Disulfide linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 12 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: 10-14 kDa, under 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 Acetonitrile and TFA with Trehalose.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

Notes

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

Alternate Names for Recombinant Human/Mouse/Rat GDF-8/Myostatin 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 member of the TGF-beta superfamily that is expressed specifically in developing and adult skeletal muscle. GDF-8 cDNA encodes a 376 amino acid (aa) prepropeptide with a 24 aa residue signal peptide, a 223 aa residue amino-terminal propeptide, and a 109 aa residue carboxy-terminal mature protein. Mature GDF-8 contains the canonical 7-cysteine motif common to other TGF-beta superfamily members. Similar to the TGF‑ beta s, activins and BMP-11, GDF-8 also contains one extra pair of cysteine residues that is not found in other family members. The bioactive form of GDF-8 is a homodimer with an apparent molecular weight of approximately 25 kDa. GDF-8 is highly conserved across species. At the amino acid sequence level, mature human, mouse, rat and cow GDF-8 are 100% identical. Within the TGF-beta superfamily, GDF-8 is most closely related to BMP-11, a mammalian protein that acts as a dorsal mesoderm and neural inducer in Xenopus explants. The two proteins share 90% amino acid sequence identity within their mature chain. A targeted disruption of GDF-8 in mouse results in large mice with a widespread increase in skeletal muscle mass, indicating that GDF-8 is a negative regulator of skeletal muscle growth. A mutation in the bovine GDF-8 gene has been shown to be responsible for the double-muscled phenotype in cattle breeds such as Belgian Blue cattle that is characterized by an increase in muscle mass. GDF-8 has also been shown to inhibit preadipocyte differentiation to adipocytes. Mature GDF-8 binds to activin type II receptors and the binding is antagonized by the activin-binding protein, follistatin. R&D Systems recombinant GDF-8 preparations have been shown to act similarly to Activin A in both the Xenopus animal cap and the K562 assays.

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2. Sharma, M. et al. (1999) J. Cell Physiol. 180:1.
3. McPherron, A.C. et al. (1997) Nature 387:83.
4. Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9306.
5. Kim, H.S. et al. (2001) Biochem. Biophys. Res. Commun. 281:902.

Bioinformatics

• Uniprot:
  • O14793.1()