Recombinant human laforin expressed in insect cells: Expression, purification, and biochemical characterizations

Abstract

A study was conducted to investigate the application of baculovirus/insect cell expression system in the production of wild-type and phosphatase active site mutant where Laforin proteins were expressed in insect cells using baculovirus and compared with that from the E. coli expression system. The phosphatase activities of purified recombinant Laforin against various substrates such as pNPP, OMFP, and glycogen were examined. The Laforin coding DNA sequence was cloned into bacterial expression vector and expressed in E. coli. The polyhistidine-tagged Laforin was also cloned into baculoviral transfer vector pVL1393, using this construct.