Differential expression profiling of recombinant bovine inhibin-Alpha at reduced temperature

The molecular biology approach for production of recombinant applied products in heterologous systems such as prokaryotes and eukaryotes is becoming a method of choice in the post genomics era. Many heterologous expression systems are available such as insects, yeast, mammalian cells however, Escherichia coli is most desirable host but the main drawback associated with expression of recombinant proteins in E. coli is production of insoluble and/or nonfunctional proteins. Earlier, effort was made to produce recombinant inhibin alpha protein to be used as fecundity vaccine in small ruminants. The bovine inhibin alpha immunogenic region of about 134 amino acid region was targeted for high level expression in E.coli but expression at 37°C resulted in high level of inclusion bodies though yield of purified protein was satisfactory. In the present study, reduced temperature (22°C) with different time intervals were investigated for the expression of soluble recombinant bINH-α aiming at improving and facilitating recombinant bINH-α protein production and purification from E. coli and to characterize it by immunological techniques.