Prokaryotic Expression and Purification of Functional Domain Coding Gene of Swine Myostatin
Daxin Pang
Abstract
Daxin Pang
Abstract
According to the gene of swine myostatin,a pair of primers were designed to amplify the functional domain coding gene of swine myostatin.The PCR product was cloned into pGEM-T vector.The sequence analysis demonstrated that the cloning sequence was the functional domain coding gene of swine myostatin.The recombinant cloning vector was digested by BamH Ⅰ and EcoR Ⅰ.The gene fraction was cloned into the expression plasmid pGEX-4T-1 and the recombinant plasmid was transformed into the competent cell of BL21(DE3).Induced by IPTG,the recombinant proteins of swine myostatin were at a level approximately 18% of total soluble proteins.
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According to the gene of swine myostatin,a pair of primers were designed to amplify the functional domain coding gene of swine myostatin.The PCR product was cloned into pGEM-T vector.The sequence analysis demonstrated that the cloning sequence was the functional domain coding gene of swine myostatin.The recombinant cloning vector was digested by BamH Ⅰ and EcoR Ⅰ.The gene fraction was cloned into the expression plasmid pGEX-4T-1 and the recombinant plasmid was transformed into the competent cell of BL21(DE3).Induced by IPTG,the recombinant proteins of swine myostatin were at a level approximately 18% of total soluble proteins.
Key concepts: Recombinant DNA, Myostatin, Gene, Cloning (programming), Coding region, Plasmid, Biology, Molecular biology