{"id":8304,"date":"2016-10-19T16:29:57","date_gmt":"2016-10-19T14:29:57","guid":{"rendered":"https:\/\/news.embl.de\/?p=8304"},"modified":"2024-03-25T10:13:48","modified_gmt":"2024-03-25T09:13:48","slug":"multibactag-protein-production-platform","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/","title":{"rendered":"MultiBacTAG: A protein production platform"},"content":{"rendered":"\n<p>Scientists can now conveniently produce recombinant eukaryotic proteins with synthetic amino-acids inserted at specific locations, thanks to a platform developed by EMBL\u2019s Edward Lemke and colleagues in an international collaboration. The wide range of applications of this new platform, called MultiBacTAG, is demonstrated in a <em>Nature Methods<\/em> paper published today.<\/p>\n\n\n\n<p>MultiBacTAG\u2019s applications include glycoengineering proteins compatible with human tissue studies, fluorescence labelling of specific targets to measure structure and dynamics in proteins, and amino acid cross-linking in order to map protein binding interfaces.<\/p>\n\n\n\n<p>Lemke anticipates that the platform will provide more insight into how specific protein complexes function, as well as possibilities to custom-design proteins for therapeutic biotechnology and pharmaceutical applications. In their paper, for example, the team used MultiBacTAG to engineer Herceptin \u2013 an antibody that associates with cancer cells \u2013 to recognise breast cancer cells in human tissue.<\/p>\n\n\n\n<p>To create MultiBacTAG, Lemke\u2019s team combined MultiBac with genetic code expansion (GCE). MultiBac is a recombinant protein production platform previously developed by Imre Berger, formerly a group leader at EMBL. Genetic code expansion (GCE), on another hand, allows scientists to reprogram a protein of interest to incorporate unnatural amino acids at specific sites in its sequence.<\/p>\n\n\n\n<p>With the support of EMBL\u2019s technology transfer arm, EMBLEM, the scientists have submitted a patent application for MultiBacTAG. The platform\u2019s development included a number of EMBL collaborators, including the labs of <a href=\"http:\/\/www.embl.de\/research\/units\/cbb\/jechlinger\">Martin Jechlinger<\/a> and <a href=\"http:\/\/www.embl.de\/research\/units\/genome_biology\/korbel\">Jan Korbel<\/a>, and the institute\u2019s <a href=\"http:\/\/www.embl.de\/services\/core_facilities\/genecore\">Genomics Core Facility<\/a> and <a href=\"http:\/\/www.embl.de\/services\/core_facilities\/pepcore\">Protein Expression and Purification Core Facility<\/a>.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>New platform useful for studies of protein binding, human tissue and more<\/p>\n","protected":false},"author":39,"featured_media":8307,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[54,43,49,69],"embl_taxonomy":[],"class_list":["post-8304","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-chemical-biology","tag-heidelberg","tag-interdisciplinary","tag-methods"],"acf":{"article_intro":"<p>New platform useful for studies of protein binding, human tissue and more<\/p>\n","related_links":[{"link_description":"Lemke lab","link_url":"http:\/\/www.embl.de\/research\/units\/scb\/lemke\/index.html"},{"link_description":"Edward Lemke on genetic code expansion","link_url":"https:\/\/news.embl.de\/science\/1408_gene_expansion\/"}],"article_sources":[{"source_description":"<p>Koehler C\u00a0<em>et al<\/em>.\u00a0<em>Nature Methods<\/em>, published online\u00a017 October 2016. DOI:\u00a010.1038\/nmeth.4032<\/p>\n","source_link_url":"http:\/\/dx.doi.org\/10.1038\/nmeth.4032"}],"vf_locked":false,"featured":false,"color":"#007B53"},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>MultiBacTAG: A protein production platform | EMBL<\/title>\n<meta name=\"description\" content=\"New MultiBacTAG platform allows scientists to conveniently produce recombinant eukaryotic proteins with synthetic amino-acids inserted at specific locations\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"MultiBacTAG: A protein production platform | EMBL\" \/>\n<meta property=\"og:description\" content=\"New MultiBacTAG platform allows scientists to conveniently produce recombinant eukaryotic proteins with synthetic amino-acids inserted at specific locations\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2016-10-19T14:29:57+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-25T09:13:48+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2016\/10\/1610-multibactag-ib.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"425\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Margaux Phares\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@mxphares\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Margaux Phares\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"1 minute\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/\"},\"author\":{\"name\":\"Margaux Phares\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/d1fced3e1bf469536cf90385bd640f83\"},\"headline\":\"MultiBacTAG: A protein production platform\",\"datePublished\":\"2016-10-19T14:29:57+00:00\",\"dateModified\":\"2024-03-25T09:13:48+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/\"},\"wordCount\":254,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/multibactag-protein-production-platform\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2016\/10\/1610-multibactag-ib.jpg\",\"keywords\":[\"chemical biology\",\"heidelberg\",\"interdisciplinary\",\"methods\"],\"articleSection\":[\"Science\",\"Science &amp; 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