Growth differentiation Factor 8 (GDF-8), also known as myostatin, is a secreted 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. GDF-8 belongs to the transforming growth factor beta (TGF-beta) superfamily, which includes the TGF-betas, bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), activins, inhibins, leftys, nodal, Mullerian inhibitory substance (MIS) and the glial cell line-derived neurotrophic factors (GDNFs). All TGF-β superfamily members are synthesized and secreted as a homodimeric prepropeptide that is cleaved by proprotein convertases such as furin to generate the dimeric N-terminal propeptide and the dimeric C-terminal mature active protein. The C-terminal mature protein contains the characteristic conserved cysteine residues involved in the formation of the cysteine knot domain. Mouse GDF-8 cDNA encodes a 376 amino acid residue (aa) preproprotein with a putative 24 aa signal peptide, a 243 aa propeptide and a 109 aa mature protein. As is the case with most TGF-beta family proteins, GDF-8 is highly conserved across species. Mature human, mouse, rat, and cow GDF-8 share 100% aa sequence identity. Among TGF-beta family members, GDF-8 is most closely related to GDF- 11/BMP-11. The two proteins share 65% overall aa sequence, within their mature regions, the two proteins differ only by 11 aa.residues. Similarly to TGF-beta-1, 2, and 3, the GDF-8 homodimeric propeptide and mature protein remained non- covalently linked after proteolytic cleavage, and is released as a biologically inactive latent complex that does bind its receptor. In serum, GDF-8 has also been found to exist in a large latent complex that also included FLGR (follistatin-related gene) and GASP-1 (growth and differentiation factor- associated serum protein-1) in addition to the propeptide. Recombinant GDF-8 propeptide is capable of associating with the active GDF-8 with high-affinity to reconstitute the latent complex and is potent GDF-8 antagonist.
Alternative Names
Growth differentiation factor 8 ; GDF-8 ; MSTN
Quantity
100 µg
Regulatory
RUO
Source
E. coli
Host
Human
Endotoxin Level
<1.0 EU/μg of recombinant protein as determined by the LAL method.
Biological Activity Comment
The ED(50) was determined by the dose-dependent proliferation inhibition of human MPC-11 cells was found to be in the range of 20-40 ng/mL.
Weight
13.0 kDa
Description
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Format
Lyophilized PowderRecombinant Myostatin was lyophilized from a 0.2 μm filtered Tris solution pH 8.0.
Purity
>95% as determined by SDS-PAGE
Storage
The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.