1998
DOI: 10.1016/s0022-1759(98)00115-x
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Isolation of single chain antibody fragments with specificity for cell surface antigens by phage display utilizing internal image anti-idiotypic antibodies

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Cited by 19 publications
(12 citation statements)
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“…Monoclonal antibodies are now considered an epochal breakthrough in medicine and are suitable as experimental tools, diagnostic reagents in therapeutics. 26,27) The advantage of phage display demonstrates a rapid and efficient strategy to generate antigen-specific monoclonal antibodies, surpassing hybridoma technology. Herein, we present the results of the library construction and selection of phage display recombinant mAbs derived from pyrethrinimmunized mice.…”
Section: Discussionmentioning
confidence: 99%
“…Monoclonal antibodies are now considered an epochal breakthrough in medicine and are suitable as experimental tools, diagnostic reagents in therapeutics. 26,27) The advantage of phage display demonstrates a rapid and efficient strategy to generate antigen-specific monoclonal antibodies, surpassing hybridoma technology. Herein, we present the results of the library construction and selection of phage display recombinant mAbs derived from pyrethrinimmunized mice.…”
Section: Discussionmentioning
confidence: 99%
“…Generation and purification of the CD30-specific single-chain antibody HRS3 scFv and the recombinant CD30-human Fc fusion protein were described earlier. [10][11][12] The anti-HRS3 idiotypic mAb 9G10 and the recombinant CD30-human Fc fusion protein were previously described.…”
Section: Antibodies and Reagentsmentioning
confidence: 99%
“…9 To counteract the Th2 polarization in Hodgkin's disease, we generated 2 recombinant anti-CD30 antibody-cytokine fusion proteins to target IL2 and IL12 to CD30 þ H/RS cells. The antibody-cytokine fusion proteins consist of the anti-CD30 single-chain fragment (scFv) antibody HRS3 10 that is linked either to the N-terminus of IL2 or to the p40 subunit of single-chain IL12. Here we demonstrate that both the anti-CD30-scFv-IL2 and the anti-CD30-scFv-IL12 fusion protein bind specifically to CD30 and retained functional cytokine activity in vitro, i.e., activation of resting NK cells to lysis of CD30 þ Hodgkin's lymphoma cells.…”
mentioning
confidence: 99%
“…ScFvs can not only be isolated against antigen but also using monoclonal antiidiotypic antibodies, which mimic cell surface receptors. The feasibility of this approach was demonstrated in a model system with an anti-CD30 scFv and antiidiotypic monoclonal antibodies that carry an internal image of an epitope of membrane-bound CD30, an antigen overexpressed on Hodgkin's lymphoma cells (Hombach et al, 1998).…”
Section: Selection Of Single-chain Fv Fragments From Phage Libraries mentioning
confidence: 99%