Recombinant Human Glycerol-3-phosphate dehydrogenase, mitochondrial (GPD2)

To produce the recombinant human glycerol-3-phosphate dehydrogenase, mitochondrial (GPD2) in the E. coli expression system, the gene fragment encoding the full-length mature GPD2 protein (43-727aa) is cloned into an appropriate expression vector. The vector also incorporates an N-terminal 6xHis-tag downstream of the gene fragment. The resulting recombinant plasmid is then introduced into E. coli host cells through a transformation process and the transformed cells are selected using suitable markers. The transformed E. coli cells are subsequently cultivated in a growth medium optimized for protein expression. To induce protein production, an inducer molecule like IPTG is added to the culture. Following an incubation period, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant GPD2 protein. Through SDS-PAGE analysis, the purified recombinant human GPD2 protein demonstrates a high purity level of up to 90%, evident by its migration as a distinct band with a molecular weight of approximately 90 kDa on the gel.