In the E. coli expression system, the recombinant human glycerol-3-phosphate dehydrogenase, mitochondrial (GPD2), is synthesized by incorporating the gene fragment encoding the full-length mature human GPD2 protein (43-727aa) into a suitable expression vector. The expression vector includes an N-terminal 10xHis-tag and a C-terminal Myc-tag downstream of the gene fragment to facilitate the purification and detection of the recombinant GPD2 protein. The constructed recombinant plasmid is then introduced into E. coli host cells via transformation, and selection is performed using appropriate markers to ensure the presence of the recombinant plasmid. The transformed E. coli cells are cultured in a growth medium optimized for protein expression, and induction of protein production is achieved by adding IPTG as an inducer. Following a suitable incubation period, the cells are harvested and lysed, releasing the intracellular contents containing the expressed recombinant GPD2 protein. The purification process allows for the isolation of the recombinant protein, which exhibits a high purity level of up to 90% as determined by SDS-PAGE analysis.<\/p>\n","protected":false},"featured_media":0,"comment_status":"open","ping_status":"closed","template":"","meta":{"_acf_changed":false},"product_brand":[],"product_cat":[168834,18],"product_tag":[26646],"class_list":["post-108617","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-gpd2","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"\n