RESUMEN
Background: Luteinizing hormone [LH] was secreted by the stimulating cells of the testes and ovaries in the anterior pituitary gland. The application of this hormone is in the treatment of men and women with infertility and amenorrhea respectively
Materials and Methods: In the present study the alpha and beta subunits of human LH gene were cloned into the pEGFP-N1 expression vector and produced the recombinant LH hormone in Chinese hamster ovary [CHO] eukaryotic system
Results: Alpha and beta subunits of LH hormone were cloned between NheI and BamHI cut sites of pEGFP_N1 expression plasmid and confirmed by PCR. Hormone expression was evaluated in CHO cell line by Western blotting using the specific antibody
Conclusion: Alpha and beta subunits of LH hormone were expressed in CHO cell line perfectly
RESUMEN
Influenza virus is the major cause of lower respiratory tract illnesses on the worldwide. Vaccination can be an effective tool to prevent its outbreak. Highly conserved viral nucleoprotein is an effective vaccine candidate to provide heterosubtypic immunity, offering resistance against various influenza virus strains. In present research NP gene was inserted in pET-22b expression vector. New construct [pET-22b/NP] was transformed into E. coli BL21 [DE3] strain and the expression of nucleoprotein was induced by IPTG. It was analyzed by SDS-PAGE and confirmed by Western blotting. Western blotting confirmed the expression and production of recombinant Influenza nucleoprotein. These results suggest that the codon-optimized influenza A virus NP gene can be efficiently expressed in E. coli