Myostatin (GDF8, MSTN) belongs to the transforming growth factor β (TGFBs) superfamily, which includes: TGF-βs, the bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), activins and inhibins. As other members of this superfamily, it is 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. Myostatin is one of the most important proteins that controls myoblast proliferation and it is a potent negative regulator of skeletal muscle mass in a number of animal species. Several studies have shown that Myostatin could play an important role in cardiac development and physiology. Genetic deletion of Myostatin or in vivo administration of the Myostatin propeptide induces muscle hypertrophy as well as enhanced glucose utilization and insulin sensitivity and a reduction in overall fat mass. Recombinant human Myostatin is a homodimer polypeptide chain containing 2x109 amino acids (267–375 of O14793 Growth/differentiation factor 8) and a 6XHistidine-based tag. It has a predicted molecular mass of 26.8 kDa (13.4 kDa under reducing conditions in SDSPAGE). Human recombinant Myostatin expressed in Nicotiana benthamiana is produced by transient expression in non-transgenic plants and is purified by sequential chromatography (FPLC). This product does not contain any animal–derived components or impurities.
Human MSTN expressed in Nicotiana benthamiana
CAT# CSC-CTK0468-5 (5 μg); CAT# CSC-CTK0468-25 (25 μg)
Greater than 97% as determined by SDS-PAGE analysis.
rHu Myostatin is fully biologically active when compared to standards. The biological activity of Myostatin is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. An ED50 30-40 ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.
Less than 0.04 EU/μg.
Lyophilized from a concentrated, sterile protein so lution containing 50 mM Tris-HCl, 1.5 M Urea, 0.004 M PMSF and 50 mM Glycine (pH 8.0).
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 50 μg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use. At higher concentrations the solubility may be reduced and multimers generated. Optimal concentration should be determined for specific application and cell lines.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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