en زیست شناسی ملکولی Molecular Biology مقالات اصلی Original Article <div style="text-align: justify;"><strong><em>Background:</em></strong> Inclusion body formation in <em>E. coli</em> is a significant problem in recombinant protein production. The aim of this study was to improve the solubility of recombinant bovine sex determining region Y protein (SRY) in BL21 (DE3) <em>E. coli</em> cells.<br> <strong><em>Methods:</em></strong> In this research two recombinant bovine SRY (rbSRY) sequences were analyzed; these were wild-type SRY (wtbSRY) and codon-optimized SRY (cobSRY). Their expression in various culture conditions was examined; these differences included IPTG concentrations, temperatures, and media stabilizers.<br> <strong><em>Results:</em></strong> IPTG and temperature significantly affected rbSRY solubility (P < 0.001). The optimum IPTG concentration and temperatures for wtbSRY and cobSRY induction were 0.3 mM at 27 and 32 &deg;C, respectively. In addition, arginine and sorbitol concentrations significantly affected rbSRY solubility (P < 0.01). Solubility of rbSRY protein was highest from the cobSRY construct in the presence 0.2 M arginine and 0.3 M sorbitol. The highest inclusion body production occurred with high glucose concentrations.<br> <strong><em>Conclusions:</em></strong> We found that modifications in temperature and IPTG and stabilizer concentrations affected rbSRY solubility.<br> &nbsp;</div> Cobsry, Inclusion Bodies, Recombinant Bovine SRY Protein, Solubility, Wtbsry. 227 235 http://rbmb.net/browse.php?a_code=A-10-293-1&slc_lang=en&sid=1 Bijan Soleymani bijan.soleymani@kums.ac.ir 100319475328460017329 100319475328460017329 No Medical Biology Research Center, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran. Ali Mostafaie amostafaie@kums.ac.ir 100319475328460017330 100319475328460017330 Yes Medical Biology Research Center, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.