<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Romani C</submitter><funding>NCI NIH HHS</funding><pagination>34617-28</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4741477</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>6(33)</volume><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</pubmed_abstract><journal>Oncotarget</journal><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.</pubmed_title><pmcid>PMC4741477</pmcid><funding_grant_id>R01 CA154460</funding_grant_id><funding_grant_id>U01 CA176067</funding_grant_id><funding_grant_id>U01 CA176067-01A1</funding_grant_id><funding_grant_id>R01 CA154460-01</funding_grant_id><pubmed_authors>Cocco E</pubmed_authors><pubmed_authors>Bignotti E</pubmed_authors><pubmed_authors>Pecorelli S</pubmed_authors><pubmed_authors>Ravaggi A</pubmed_authors><pubmed_authors>Romani C</pubmed_authors><pubmed_authors>Santin AD</pubmed_authors><pubmed_authors>Bugatti A</pubmed_authors><pubmed_authors>Odicino FE</pubmed_authors><pubmed_authors>Tassi R</pubmed_authors><pubmed_authors>Mitola S</pubmed_authors><pubmed_authors>Sartori E</pubmed_authors><pubmed_authors>Bandiera E</pubmed_authors><pubmed_authors>Zanotti L</pubmed_authors><pubmed_authors>de Marco A</pubmed_authors><pubmed_authors>Moratto D</pubmed_authors><pubmed_authors>Todeschini P</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Oct</publication><modification>2026-05-05T11:59:21.219Z</modification><creation>2019-03-27T02:08:24Z</creation></dates><accession>S-EPMC4741477</accession><cross_references><pubmed>26416446</pubmed><doi>10.18632/oncotarget.5315</doi></cross_references></HashMap>