{"doi":"10.1096/fasebj.22.2_supplement.255","title":"Affinity Purification of Tag‐free Recombinant Proteins in Under an Hour Using the Profinity eXact™ Purification System","abstract":"<jats:p>The use of affinity tags has greatly simplified the purification of recombinant proteins. However, the presence of the affinity tag in the purified protein can interfere with the protein's biological function or downstream application, and removal of the tag is necessary. Tag removal methods often utilize tagged endoproteases to cleave a peptide sequence engineered between the tag and the target protein. The drawbacks of this process are that these proteases often require extended incubation times, require a subsequent affinity purification step to be removed, are expensive, and may leave the final tag‐free target protein with additional amino acid residues at the protein terminus. Utilizing a small 8kD affinity tag and its immobilized mutant subtilisin binding partner, the novel Profinity eXact purification system affords a rapid one‐step integrated purification‐cleavage protocol for recombinant protein production that avoids the complications associated with conventional purification and tag removal procedures. An overview of the Profinity eXact system will be presented, including representative Profinity eXact tag purifications.</jats:p>","journal":"The FASEB Journal","year":2008,"id":600653,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":530833,"name":"Xuemei He","orcid":"0000-0003-3516-1800","position":1,"is_corresponding":false},{"id":1539959,"name":"Natalia Oganesyan","orcid":null,"position":2,"is_corresponding":false},{"id":230905,"name":"Lei Li","orcid":"0000-0002-4485-1937","position":3,"is_corresponding":false},{"id":1539962,"name":"Shane Petersen","orcid":null,"position":4,"is_corresponding":false},{"id":1539964,"name":"Marie Nguyen","orcid":null,"position":5,"is_corresponding":false},{"id":1539965,"name":"Lily Woo","orcid":null,"position":6,"is_corresponding":false},{"id":1539966,"name":"William Strong","orcid":null,"position":7,"is_corresponding":false},{"id":1539955,"name":"Dennis C. 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Utilizing a small 8kD affinity tag and its immobilized mutant subtilisin binding partner, the novel Profinity eXact purification system affords a rapid one‐step integrated purification‐cleavage protocol for recombinant protein production that avoids the complications associated with conventional purification and tag removal procedures. An overview of the Profinity eXact system will be presented, including representative Profinity eXact tag purifications.</jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"21097893","pmcid":null,"openalex_id":"https://openalex.org/W121648514","authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1096%2Ffasebj.22.2_supplement.255","host_type":"publisher"},{"url":"http://onlinelibrary.wiley.com/wol1/doi/10.1096/fasebj.22.2_supplement.255/fullpdf","host_type":"publisher"},{"url":"https://doi.org/10.1096/fasebj.22.2_supplement.255","host_type":"journal"}],"fields_of_study":["Transgenic Plants and Applications","Protein purification and stability","Enzyme Production and Characterization"],"mesh_terms":[],"keywords":["FLAG-tag","Tandem affinity purification","Recombinant DNA","Proteases","Affinity chromatography","Cleave","Myc-tag","Biochemistry","Protein purification","Target protein","Protein tag","Subtilisin","Chemistry","Downstream processing","Chromatography","Biology","Enzyme","Fusion protein","Gene"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Zero hunger"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T13:44:54.223049Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}