In the E. coli expression system, the recombinant human glucose-6-phosphatase (G6PC) with an N-terminal 6xHis-SUMO-tag is synthesized by cloning the gene fragment encoding the 82-117aa of the human G6PC protein into a suitable expression vector. The N-terminal 6xHis-SUMO-tag is also inserted into the vector downstream of the desired gene fragment. The constructed recombinant plasmid is introduced into E. coli host cells through a transformation process. The transformed cells are selected using appropriate markers, ensuring the presence of the recombinant plasmid. Subsequently, the transformed E. coli cells are cultured in a growth medium optimized for protein expression. Induction of protein expression is achieved by adding an inducer molecule, such as IPTG. Following an incubation period, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant G6PC protein. The purified recombinant human G6PC protein exhibits a purity level of up to 85% as determined by SDS-PAGE analysis. On the gel, the protein migrates as a band with a molecular weight of approximately 20 kDa.<\/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":[33735],"class_list":["post-108621","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-g6pc1","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"\n