Key result
A pET-lipasin prokaryotic recombinant expression vector was successfully constructed, yielding a 25.2-kDa porcine lipasin protein to facilitate further biological function research.
This study successfully cloned and expressed the porcine lipasin gene, providing a basis for further research on its biological function in lipid metabolism.
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Enables further porcine lipasin studies in lipid metabolism; leaves open any clinical relevance for human cardiovascular disease.
Lipasin has recently been demonstrated to be involved in lipid metabolism. In this study, two specific primers were used to amplify the lipasin open reading frame from porcine liver tissue. The polymerase chain reaction product was cloned to a pGEM®-T Easy Vector, digested by SalI and NotI, and sequenced. The lipasin fragment was then cloned to a pET21(b) vector and digested by the same restriction enzyme. The recombinant plasmid was transferred to Escherichia coli (BL21), and the lipasin protein was induced with isopropyl-β-D-thiogalactopyranoside. The protein obtained was identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting. A pET-lipasin prokaryotic recombinant expression vector was successfully constructed, and a 25.2-kDa protein was obtained. This study provides a basis for further research on the biological function of porcine lipasin.
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Li et al. (2015) studied this question. Cloning and prokaryotic expression of porcine lipasin gene was evaluated on Construction of expression vector and protein expression. A pET-lipasin prokaryotic recombinant expression vector was successfully constructed, yielding a 25.2-kDa porcine lipasin protein to facilitate further biological function research.
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