In the E. coli expression system, the recombinant human protein phosphatase 1 regulatory subunit 3G (PPP1R3G) is generated by introducing the gene fragment encoding the full-length PPP1R3G protein (1-358aa) into a suitable expression vector. This expression vector is designed to include an N-terminal 10xHis-tag and a C-terminal Myc-tag downstream of the gene fragment, enabling convenient purification and detection of the recombinant protein. Following the transformation of the recombinant plasmid into E. coli host cells and selection using appropriate markers, the transformed cells are cultured in a growth medium optimized for protein expression. Recombinant protein production is induced by the addition of IPTG as an inducer. After an appropriate incubation period, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant PPP1R3G protein. The purification process involves isolating the recombinant protein, which exhibits a high purity level of up to 85% as confirmed 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":[133704],"class_list":["post-108436","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-ppp1r3g","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"\n