In the E. coli expression system, the production process of the recombinant human Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) (T253M, Q257L) tagged with an N-terminal 6xHis-tag involves several steps. The gene fragment encoding the full-length mature human PTPN11 protein (2-593aa), including the T253M and Q257L mutations, is cloned into a suitable expression vector. The vector is designed to incorporate an N-terminal 6xHis-tag downstream of the gene fragment, allowing for convenient purification and detection of the recombinant protein. The constructed recombinant plasmid is transformed into E. coli host cells and transformed cells are selected and cultured in a growth medium optimized for recombinant protein expression. Following an appropriate incubation period, the cells are harvested and lysed to release the intracellular contents, including the expressed recombinant PTPN11 protein. The purity of the purified recombinant PTPN11 protein is assessed using SDS-PAGE analysis, measuring up to 90%.<\/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":[19089],"class_list":["post-108586","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-ptpn11","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"\n