{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Romani C"],"funding":["NCI NIH HHS"],"pagination":["34617-28"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4741477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(33)"],"pubmed_abstract":["Membrane protein claudin3 has been recently suggested as a marker for biologically aggressive tumors and a possible target for the therapeutic delivery of active anti-cancer compounds. Claudin3-binding molecules such as the Clostridium perfringens enterotoxin (CPE), CPE-related molecules, and murine and chimeric antibodies have shown promising antitumor efficacy in preclinical oncological settings. We first engineered a fully human anti-claudin3 IgG1 antibody (IgGH6) by fusing the human IgG1 Fc-domain to the anti-claudin3 scFvH6 previously isolated from a pre-immune phage display library. The construct was expressed in mammalian cells and specifically targeted claudin3 endogenously expressed on the surface of different human ovarian cancer cell lines. No detectable cross-reactivity with ot"],"journal":["Oncotarget"],"pubmed_title":["Evaluation of a novel human IgG1 anti-claudin3 antibody that specifically recognizes its aberrantly localized antigen in ovarian cancer cells and that is suitable for selective drug delivery."],"pmcid":["PMC4741477"],"funding_grant_id":["R01 CA154460","U01 CA176067","U01 CA176067-01A1","R01 CA154460-01"],"pubmed_authors":["Cocco E","Bignotti E","Pecorelli S","Ravaggi A","Romani C","Santin AD","Bugatti A","Odicino FE","Tassi R","Mitola S","Sartori E","Bandiera E","Zanotti L","de Marco A","Moratto D","Todeschini P"],"additional_accession":[]},"is_claimable":false,"name":"Evaluation of a novel human IgG1 anti-claudin3 antibody that specifically recognizes its aberrantly localized antigen in ovarian cancer cells and that is suitable for selective drug delivery.","description":"Membrane protein claudin3 has been recently suggested as a marker for biologically aggressive tumors and a possible target for the therapeutic delivery of active anti-cancer compounds. Claudin3-binding molecules such as the Clostridium perfringens enterotoxin (CPE), CPE-related molecules, and murine and chimeric antibodies have shown promising antitumor efficacy in preclinical oncological settings. We first engineered a fully human anti-claudin3 IgG1 antibody (IgGH6) by fusing the human IgG1 Fc-domain to the anti-claudin3 scFvH6 previously isolated from a pre-immune phage display library. The construct was expressed in mammalian cells and specifically targeted claudin3 endogenously expressed on the surface of different human ovarian cancer cell lines. No detectable cross-reactivity with ot","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2026-05-05T11:59:21.219Z","creation":"2019-03-27T02:08:24Z"},"accession":"S-EPMC4741477","cross_references":{"pubmed":["26416446"],"doi":["10.18632/oncotarget.5315"]}}