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Merck

Effect of antibody modifications on its biomolecular binding as determined by surface plasmon resonance.

Analytical biochemistry (2011-11-19)
Sandeep Kumar Vashist
ABSTRAKT

A surface plasmon resonance (SPR)-based procedure was developed to determine the effect of antibody modifications on its biomolecular binding behavior. Mouse immunoglobulin G (IgG) was immobilized on a protein A-functionalized gold-coated SPR chip. Goat anti-mouse IgG and its various commercially available modifications (i.e., conjugated with atto 550, atto 647, tetramethylrhodamine isothiocyanate [TRITC], horseradish peroxidase [HRP], or biotin) were employed in exactly the same concentration for the detection of mouse IgG. The various modifications of goat anti-mouse IgG decreased its biomolecular binding to mouse IgG in the order of unmodified>HRP-labeled>atto 550-labeled>biotinylated>TRITC-labeled>atto 647-labeled.

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Sigma-Aldrich
Atto 647 NHS ester, BioReagent, suitable for fluorescence, ≥90% (HPLC)
Sigma-Aldrich
Atto 550 NHS ester, BioReagent, suitable for fluorescence
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Atto 647 maleimide, BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)
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Atto 550 Protein Labeling Kit, BioReagent, suitable for fluorescence
Sigma-Aldrich
Atto 550, for fluorescence, ≥90% (HPLC)