<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ma L</submitter><funding>NIDDK NIH HHS</funding><pagination>857-64</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4954766</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>37(6)</volume><pubmed_abstract>&lt;h4>Aim&lt;/h4>Nanobody is an antibody fragment consisting of a single monomeric variable antibody domain, which can be used for a variety of biotechnological and therapeutic purposes. The aim of this work was to isolate and characterize a human signal domain antibody against VEGFR-2 domain3 (VEGFR D3) from a phage display library.&lt;h4>Methods&lt;/h4>To produce antigen-specific recombinant nanobodies with high affinity to VEGFR2 D3, a liquid phase panning strategy was used for all rounds of panning. For nanobody expression and purification, four VEGFR2 D3-blocking clones were subcloned into a pETduet-biotin-MBP expression vector. The recombinant proteins carried an MBP tag to facilitate purification by affinity chromatography. Recombinant NTV(1-4) was obtained after an additional gel filtration c</pubmed_abstract><journal>Acta pharmacologica Sinica</journal><pubmed_title>Generation and characterization of a human nanobody against VEGFR-2.</pubmed_title><pmcid>PMC4954766</pmcid><funding_grant_id>R01 DK071662</funding_grant_id><pubmed_authors>Jiang Y</pubmed_authors><pubmed_authors>Wang M</pubmed_authors><pubmed_authors>Ma L</pubmed_authors><pubmed_authors>Chen XT</pubmed_authors><pubmed_authors>Zhang J</pubmed_authors><pubmed_authors>Melcher K</pubmed_authors><pubmed_authors>Gu K</pubmed_authors><pubmed_authors>Zhang CH</pubmed_authors><pubmed_authors>Xu HE</pubmed_authors></additional><is_claimable>false</is_claimable><name>Generation and characterization of a human nanobody against VEGFR-2.</name><description>&lt;h4>Aim&lt;/h4>Nanobody is an antibody fragment consisting of a single monomeric variable antibody domain, which can be used for a variety of biotechnological and therapeutic purposes. The aim of this work was to isolate and characterize a human signal domain antibody against VEGFR-2 domain3 (VEGFR D3) from a phage display library.&lt;h4>Methods&lt;/h4>To produce antigen-specific recombinant nanobodies with high affinity to VEGFR2 D3, a liquid phase panning strategy was used for all rounds of panning. For nanobody expression and purification, four VEGFR2 D3-blocking clones were subcloned into a pETduet-biotin-MBP expression vector. The recombinant proteins carried an MBP tag to facilitate purification by affinity chromatography. Recombinant NTV(1-4) was obtained after an additional gel filtration c</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jun</publication><modification>2025-05-29T21:25:58.537Z</modification><creation>2025-05-29T21:25:58.537Z</creation></dates><accession>S-EPMC4954766</accession><cross_references><pubmed>27108602</pubmed><doi>10.1038/aps.2016.2</doi></cross_references></HashMap>