نوع فایل:PDFتعداد صفحات:سال انتشار:1395چکیدهSeveral expression hosts have been employed for the production of bone morphogenetic protein2 (BMP- 2), inducing de novo bone formation and is widely used in clinical applications. However,every expression system has its merits and demerits. For example, although Escherichia coli issimple and robust, but inept to make disulfide bond; hence, heterologous proteins are produced inthe form of inclusion bodies, entailing in vitro refolding strategies. On the other hand, yeast, whichis a lower eukaryote, is able to perform glycosylation of the recombinant proteins. However, itsglycosylation pattern is different from human beings. Ultimately, Leishmania tarentolae, a parasiteprotozoan of the lizard, unifying both the characteristics of prokaryotes and eukaryotes, has beenintroduced for the expression of glycoproteins. It is capable of making disulfide bonds, expressingcorrectly folded and biologically active recombinant proteins. In the current study, we successfullycloned and expressed proBMP-2 gene in L. tarentolae. Integration of the gene was confirmed byPCR; whereas, transcription of the coding gene was verified by back translating the target mRNA.Besides, the expression of BMP-2 was assessed by SDS-PAGE and Western blotting. A 12 kDaband was obtained, equivalent to monomeric form of BMP-2.واژگان کلیدی