Selected article for: "human IgG antibody and IgG antibody"

Author: Rogers, J.; Schoepp, R.J.; Schröder, O.; Clements, T.L.; Holland, T.F.; Li, J.Q.; Li, J.; Lewis, L.M.; Dirmeier, R.P.; Frey, G.J.; Tan, X.; Wong, K.; Woodnutt, G.; Keller, M.; Reed, D.S.; Kimmel, B.E.; Tozer, E.C.
Title: Rapid discovery and optimization of therapeutic antibodies against emerging infectious diseases
  • Document date: 2008_5_13
  • ID: xkx56h0o_36
    Snippet: The kinetics of the human and chimera antibodies were tested using surface plasmon resonance technology on a Biacore 2000. Each antibody was captured onto the sensor surface using an anti-human IgG antibody at the desired level of $200 RU. Binding of the SARS spike protein was tested at 100 and 33.3 nM as the highest concentrations for the 4049Fab14 and 2978/10 antibodies, respectively, with a 3-fold dilution series. Each sample concentration ser.....
    Document: The kinetics of the human and chimera antibodies were tested using surface plasmon resonance technology on a Biacore 2000. Each antibody was captured onto the sensor surface using an anti-human IgG antibody at the desired level of $200 RU. Binding of the SARS spike protein was tested at 100 and 33.3 nM as the highest concentrations for the 4049Fab14 and 2978/10 antibodies, respectively, with a 3-fold dilution series. Each sample concentration series was tested in duplicate. Surfaces were fully regenerated with two 30 s pulses of 1/100 dilution of phosphoric acid.

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