Binding characteristics between human IgG, the peptide and C1q protein investigated were carried out using a BIAcore X-100 instrument (GE Healthcare, Uppsala, Sweden). 3000 the resonance units (RU) human IgG was immobilized on a CM5 sensor chip (GE Healthcare) by standard amine coupling and RU were calculated based on the analyte molecular weight. In parallel, one flow cell was incubated with buffer alone (i.e. without IgG), serving as control. Interaction experiments were performed with injections of 125, 250, 500, 1000 nM of peptides in running buffer (10 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% surfactant P20, and 3.4 mM EDTA) at a flow rate of 30 μl/min. After the end of each injection, dissociation was performed with 50 mM NaOH, followed by a washing procedure. The BIA evaluation 3.1 analysis software (GE Healthcare) was used to determine equilibrium dissociation constants (KD) from the processed data sets by fitting to a 1:1 molecular binding model with drifting baseline. In another experiment C1q protein was injected over the immobilized IgG or immediately after the peptide was injected over the surface.
Bia evaluation 3.1 analysis software
Manufactured by GE Healthcare
The BIA Evaluation 3.1 analysis software is a tool designed for evaluating bioelectrical impedance (BIA) data. It provides core functionality for analyzing and interpreting BIA measurements without extrapolation or interpretation of the intended use.
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Lab products found in correlation
2 protocols using bia evaluation 3.1 analysis software
1
Quantifying IgG-Peptide-C1q Interactions
2
OPN-AMP Binding Kinetics Analysis
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Binding characteristics between OPN and the AMPs investigated were carried out using a BIAcore X-100 instrument (GE Healthcare, Uppsala, Sweden). Human OPN was immobilized on a CM5 sensor chip (GE Healthcare) by standard amine coupling and the resonance units (RU) were calculated based on the analyte molecular weight. In parallel, one flow cell was incubated with buffer alone (i.e. without OPN), serving as control. Interaction experiments were performed with injections of 31.25, 62.5, 125, 250, 500 nM of AMPs in running buffer (10 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% surfactant P20, and 3.4 mM EDTA) at a flow rate of 30 μl/min. After the end of each injection, dissociation was performed with 0.5 M NaCl for 10 min, followed by a washing procedure. After X and Y normalization of data, the blank curves from the control flow cell of each injected concentration were subtracted. The BIA evaluation 3.1 analysis software (GE Healthcare) was used to determine equilibrium dissociation constants (KD) from the processed data sets by fitting to a 1:1 molecular binding model with drifting baseline.
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