@article{MAKHILLJAVA20141374295,
    title = {Functional Characterization of Human Myostatin C-Domain Recombinant Protein and Production of Myostatin Polyclonal Antibody},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {13},
    number = {7},
    pages = {430-436},
    year = {2014},
    issn = {1680-5593},
    doi = {javaa.2014.430.436},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2014.430.436},
    author = {Changqing,Haiyan,Nou,Juan,Keke and},
    keywords = {Myostatin,recombinant protein,function characterization,polyclonal antibody,neonatal mice},
    abstract = {Myostatin (GDF-8) is a member of the Transforming Growth Factor-Beta 
  (TGF-β) superfamily that is highly expressed in skeletal muscle and myostatin 
  loss of function leads to doubling of skeletal muscle mass while dysregulated 
  myostatin activity is associated with a number of metabolic disorders including 
  muscle cachexia, obesity and type II diabetes. In this study, to further investigate 
  the application of the myostatin protein, researchers constructed and expressed 
  recombinant myostatin protein and its polyclonal antibody. The C-domain of human 
  myostatin gene was cloned into the prokaryotic expression vector pET-32a-c (+) 
  to express His-tagged myostatin-C protein and was expressed in Origami B DE3) 
  induced by IPTG. After purification, the recombinant protein was used to raise 
  the anti-myostatin polyclonal antibody. In addition, the immunogenicity of the 
  recombinant myostatin-C protein was detected by mice immunized with the protein. 
  The results showed the purity of the recombinant myostatin-C protein is >90%. 
  The final concentration is 3.5 mg mL<SUP>-1</SUP>. It reacted with the myostatin 
  antibody with a strong specific reactive band. The titer of anti-myostatin serum 
  was determined to be 1:50,000. Immunization of mice with recombinant protein 
  could significantly increase the body weight of neonatal mice and themselves. 
  These results proved that researchers obtained a high-level expression of the 
  recombinant myostatin-C protein as well as high titer of rabbit polyclonal antibody. 
  It retaining antigen-binding activity can be employed for some therapeutic use. 
  This special polyclonal antibody could provide a good tool for further studying 
  structural and functional characterization of myostatin protein.}
    }