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In JoVE (1)
Other Publications (3)
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Articles by Finn Hung in JoVE
एक उच्च throughput प्रोटीन चिकित्सा के लिए विनिर्माण सेल लाइन्स के विकास के लिए स्वचालित प्लेटफार्म
Shuangping Shi, Russ G.G. Condon, Liang Deng, Jason Saunders, Finn Hung, Yung-Shyeng Tsao, Zhong Liu
Merck Research Laboratory, Merck & Co., Inc
एक उच्च throughput, प्रोटीन चिकित्सा के उत्पादन के लिए विनिर्माण सेल लाइन के विकास के लिए स्वचालित मंच वर्णित है. बी.डी. FACS Aria सेल सॉर्टर का कार्यान्वयन, CloneSelect Imager और TECAN स्वतंत्रता EVO तरल हैंडलिंग प्रणाली सेल लाइन के विकास में काफी वृद्धि हुई सुधार सेल लाइन गुणवत्ता और उच्च reproducibility के साथ प्रसंस्करण क्षमता का प्रदर्शन किया है.
Other articles by Finn Hung on PubMed
Journal of Chromatography. A. Jan, 2008 | Pubmed ID: 17981289
A heteropolymer (HP) is a unique dual antibody conjugate composed of specific, chemically cross-linked monoclonal antibodies (mAbs). In this study we have demonstrated that HPs can be purified using hydrophobic interaction chromatography (HIC). Two propyl HIC resins; [PolyPropyl A and EMD Fractogel Propyl (S)] were evaluated in this study. Phosphate buffers, pH 6.5 containing ammonium sulfate or sodium sulfate were used to bind the HP to the column. A descending sulfate gradient or step gradient was used to elute the bound HP species from the column. The HP reaction mixture typically contains multiple conjugated HP species, as well as unreacted monomer mAbs. Conjugated HP product was successfully separated from unreacted antibody monomers with both propyl resins using buffers with ammonium sulfate. There was no monomer separation from HP using buffers with sodium sulfate. The purification processes, presented in this study allows the non-cross-linked antibodies to pass through the column without being bound to the resin, while the cross-linked antibodies (the HP product) bound to the column were subsequently eluted by decreasing the ammonium sulfate concentration in the running buffer. HP product was efficiently separated from free mAbs using Propyl HIC resins at both analytical and preparative scales.
Biotechnology Journal. Apr, 2010 | Pubmed ID: 20222103
The productivity of stably transfected cell lines is of critical importance for the manufacturing of therapeutic proteins. Various methods have been successfully implemented to increase the production output of mammalian cell cultures. Increasing evidence suggests that optimization of the gene coding sequences of an expression vector can improve specific cell line yield of the recombinant protein. Here we demonstrate that gene optimization substantially enhances antibody production in Chinese hamster ovary cells. When gene optimization was applied to the heavy and light chain genes of a therapeutic antibody, we observed increased antibody production in transient transfection. Elevated heavy chain mRNA level was associated with the increase of antibody production. Further analysis suggested that the increased antibody expression is attributable to enhanced mRNA stability resulting from gene optimization. Gene optimization also led to increased antibody production in stable clones.