To express the recombinant human inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAHP) in E. coli, the gene fragment encoding the full-length human CMAHP protein (amino acids 1-501) and an N-terminal 10xHis-tag and C-terminal Myc-tag is cloned into a suitable expression vector. The cloning process involves ligating the gene fragment into the vector downstream of the appropriate promoter and regulatory elements. The resulting expression construct is then transformed into E. coli host cells using a transformation method. The transformed cells are selected to ensure the presence of the recombinant plasmid. Subsequently, a large-scale culture of the transformed E. coli cells is established in a growth medium under optimal conditions for protein expression. The N-terminal 10xHis-tag and C-terminal Myc-tag allow for convenient purification and detection of the recombinant CMAHP protein. The recombinant CMAHP protein can be extracted and purified from the cell lysate. The purity of the recombinant human CMAHP protein is assessed through SDS-PAGE analysis, reaching up to 90%. It migrates onto a band of 64 kDa molecular weight on the gel.<\/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":[134197],"class_list":["post-108709","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-cmahp","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"\n