{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schneider DW"],"funding":["NCI NIH HHS"],"pagination":["435-43"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4962604"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["50(3)"],"pubmed_abstract":["Unlabelled
To optimize in vivo tissue uptake kinetics and clearance of engineered monoclonal antibody (mAb) fragments for radiotherapeutic and radiodiagnostic applications, we compared the biodistribution and tumor localization of four (111)In- and (86)Y-labeled antibody formats, derived from a single antimindin/RG-1 mAb, in a prostate tumor model. The IgG, diabody, single-chain variable domain (scFv), and novel miniantibody formats, composed of the human IgE-C(H)4 and a modified IgG1 hinge linked to scFv domains, were compared.Methods
Antibodies were first derivatized with the bifunctional chelator CHX-A''-diethylenetriamine pentaacetic acid and then bound to the radiometal to create radiolabeled immunoconjugates. Human LNCaP xenografts were grown in nude mice, and (111)In"],"journal":["Journal of nuclear medicine : official publication, Society of Nuclear Medicine"],"pubmed_title":["In vivo biodistribution, PET imaging, and tumor accumulation of 86Y- and 111In-antimindin/RG-1, engineered antibody fragments in LNCaP tumor-bearing nude mice."],"pmcid":["PMC4962604"],"funding_grant_id":["R24 CA086307"],"pubmed_authors":["Light DR","Heitner T","McLean K","Schneider DW","Yoo J","Lewis JS","Parry G","Alicke B","Parry R","Satozawa N"],"additional_accession":[]},"is_claimable":false,"name":"In vivo biodistribution, PET imaging, and tumor accumulation of 86Y- and 111In-antimindin/RG-1, engineered antibody fragments in LNCaP tumor-bearing nude mice.","description":"Unlabelled
To optimize in vivo tissue uptake kinetics and clearance of engineered monoclonal antibody (mAb) fragments for radiotherapeutic and radiodiagnostic applications, we compared the biodistribution and tumor localization of four (111)In- and (86)Y-labeled antibody formats, derived from a single antimindin/RG-1 mAb, in a prostate tumor model. The IgG, diabody, single-chain variable domain (scFv), and novel miniantibody formats, composed of the human IgE-C(H)4 and a modified IgG1 hinge linked to scFv domains, were compared.Methods
Antibodies were first derivatized with the bifunctional chelator CHX-A''-diethylenetriamine pentaacetic acid and then bound to the radiometal to create radiolabeled immunoconjugates. Human LNCaP xenografts were grown in nude mice, and (111)In","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Mar","modification":"2025-04-25T22:26:57.654Z","creation":"2019-03-27T02:19:18Z"},"accession":"S-EPMC4962604","cross_references":{"pubmed":["19223400"],"doi":["10.2967/jnumed.108.055608"]}}