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Catalog #
90141
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Description
Recombinant human Myostatin is a disulfide-linked homodimeric protein consisting of two 110 amino acid residues, and migrates as an approximately 25 kDa protein under non-reducing conditions and as a 13 kDa protein under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Myostatin mature chain was expressed in E. coli.
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Synonyms
GDF8, Growth differentiation Factor 8, myostatin, MSTN
Product Info
Storage and Usage
Citations 0
Species
Human
Host Species/Expression System
E. coli
Purity
≥97% by SDS-PAGE and HPLC
Format
lyophilized protein
Formulation
Lyophilized from a 0.2 μm filtered Tris solution pH 8.0.
MW
13 kDa
Endotoxin Level
<0.1 ng/μg (1 EU/μg), using the LAL gel clot method.
Amino Acids
267–375
Biological Activity
The ED50 was determined by the dose-dependent proliferation inhibition of human MPC-11 cells to be in the range of 20.0-40.0 ng/ml.
Genbank #
O14793
UniProt #
O14793
Background
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 β (TGF-β) superfamily . 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 a.a. signal peptide, a 243 a.a. propeptide and a 109 a.a. mature protein. GDF-8 is highly conserved across species. Mature human, mouse, rat, and cow GDF-8 share 100% aa sequence identity. Among TGF-β 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 a.a. residues. Similarly to TGF-β1, 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.
References
1. LeBrasseur, N., et al. J Gerontol A Biol Sci Med Sci (2009) 64A (9): 940-948. 2. Sumner, C., et al. Hum. Mol. Genet. (2009) 18 (17): 3145-3152. 3. Rodgers, B.D., et al. October 15, 2009 The Journal of Physiology, 587, 4873-4886.
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Datasheets/Protocols
Datasheets provide protein specifications, which is non lot-specific information. Contact us to request information on currently available lots or to obtain a lot-specific data report.
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