<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Schneider DW</submitter><funding>NCI NIH HHS</funding><pagination>435-43</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4962604</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>50(3)</volume><pubmed_abstract>&lt;h4>Unlabelled&lt;/h4>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.&lt;h4>Methods&lt;/h4>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</pubmed_abstract><journal>Journal of nuclear medicine : official publication, Society of Nuclear Medicine</journal><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.</pubmed_title><pmcid>PMC4962604</pmcid><funding_grant_id>R24 CA086307</funding_grant_id><pubmed_authors>Light DR</pubmed_authors><pubmed_authors>Heitner T</pubmed_authors><pubmed_authors>McLean K</pubmed_authors><pubmed_authors>Schneider DW</pubmed_authors><pubmed_authors>Yoo J</pubmed_authors><pubmed_authors>Lewis JS</pubmed_authors><pubmed_authors>Parry G</pubmed_authors><pubmed_authors>Alicke B</pubmed_authors><pubmed_authors>Parry R</pubmed_authors><pubmed_authors>Satozawa N</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><description>&lt;h4>Unlabelled&lt;/h4>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.&lt;h4>Methods&lt;/h4>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</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 Mar</publication><modification>2025-04-25T22:26:57.654Z</modification><creation>2019-03-27T02:19:18Z</creation></dates><accession>S-EPMC4962604</accession><cross_references><pubmed>19223400</pubmed><doi>10.2967/jnumed.108.055608</doi></cross_references></HashMap>