biostudies-literatureNavas TARRA NIH HHSNational Cancer InstituteNCI NIH HHSe0199361https://www.ebi.ac.uk/biostudies/studies/S-EPMC6013203biostudies-literatureUnknown13(6)The presence of cancer stem cells (CSCs) and the induction of epithelial-to-mesenchymal transition (EMT) in tumors are associated with tumor aggressiveness, metastasis, drug resistance, and poor prognosis, necessitating the development of reagents for unambiguous detection of CSC- and EMT-associated proteins in tumor specimens. To this end, we generated novel antibodies to EMT- and CSC-associated proteins, including Goosecoid, Sox9, Slug, Snail, and CD133. Importantly, unlike several widely used antibodies to CD133, the anti-CD133 antibodies we generated recognize epitopes distal to known glycosylation sites, enabling analyses that are not confounded by differences in CD133 glycosylation. For all target proteins, we selected antibodies that yielded the expected target protein molecular weiPloS oneNovel antibody reagents for characterization of drug- and tumor microenvironment-induced changes in epithelial-mesenchymal transition and cancer stem cells.PMC6013203HHSN261200800001EContract No. HHSN261200800001EHollingshead MGDieckman LTakebe NLee YHBottaro DPColantonio SAlcoser SYNavas TDoroshow JHHiltke TWhiteley GAziz ABorgel SPfister TDKaczmarczyk JParchment RETomaszewski JEKinders RJSaul RGfalseNovel antibody reagents for characterization of drug- and tumor microenvironment-induced changes in epithelial-mesenchymal transition and cancer stem cells.The presence of cancer stem cells (CSCs) and the induction of epithelial-to-mesenchymal transition (EMT) in tumors are associated with tumor aggressiveness, metastasis, drug resistance, and poor prognosis, necessitating the development of reagents for unambiguous detection of CSC- and EMT-associated proteins in tumor specimens. To this end, we generated novel antibodies to EMT- and CSC-associated proteins, including Goosecoid, Sox9, Slug, Snail, and CD133. Importantly, unlike several widely used antibodies to CD133, the anti-CD133 antibodies we generated recognize epitopes distal to known glycosylation sites, enabling analyses that are not confounded by differences in CD133 glycosylation. For all target proteins, we selected antibodies that yielded the expected target protein molecular wei2018-01-01T00:00:00Z20182025-04-04T18:41:45.967Z2019-03-26T23:44:54ZS-EPMC60132032992806210.1371/journal.pone.0199361