Anti-variant fc region antibodies and methods of use
An antibody and antibody fragment technology, applied in chemical instruments and methods, anti-receptor/cell surface antigen/cell surface determinant immunoglobulin, anti-growth factor immunoglobulin, etc., can solve problems such as limitation
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Embodiment 1
[0575] Materials and methods
[0576] Nucleotide sequences for human immunoglobulin light and heavy chains are given in Kabat, E.A. et al., Sequences of Proteins of Immunological Interest, 5th Edition, Public Health Service, National Institutes of Health, Bethesda, MD (1991). General information. Amino acids of antibody chains are numbered and referenced according to the numbering of Kabat (Kabat, E.A. et al., Sequences of Proteins of Immunological Interest, 5th ed., Public Health Service, National Institutes of Health, Bethesda, MD (1991)).
[0577] recombinant DNA technology
[0578] DNA can be manipulated using standard methods described in Sambrook, J. et al., Molecular Cloning: A laboratory manual; Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1989. Molecular biology reagents were used according to the manufacturer's instructions.
[0579] gene synthesis
[0580] The desired gene segments can be prepared from oligonucleotides produced by chemical ...
Embodiment 2
[0627] Antibodies reported here serve as capture antibodies
[0628] Biotinylated anti-PGLALA Fc region antibodies or biotinylated anti-AAA Fc region antibodies, respectively, were bound to wells of a streptavidin-coated multi-well plate (SA-MTP) to generate capture plates. Excess unbound antibody is removed by washing. Sample / standard antibodies spiked with human and cynomolgus monkey serum (10% final concentration) were added to the wells of capture antibody-coated SA-MTP multiwell plates and incubated for 1 hour at room temperature. After washing, the wells were incubated with digoxigenylated anti-human kappa antibody M1.7.10 (see eg, WO 2011 / 048043, incorporated herein by reference). After washing, the bound digoxigenylated anti-human kappa antibody complexes were incubated with horseradish peroxidase (HRP)-labeled anti-digoxigenin antibody. After one more wash step, ABTS solution was added to the wells and incubated. The color reaction product was measured by an Elisa ...
Embodiment 3
[0663] Antibodies reported here as tracer antibodies
[0664] Biotinylated anti-human kappa antibody M1.7.10 (see eg WO 2011 / 048043) was bound to the wells of a streptavidin-coated multi-well plate (SA-MTP) to generate capture plates. Excess unbound antibody is removed by washing. Sample / standard antibodies spiked with human and cynomolgus monkey serum (10% final concentration) were added to the wells of capture antibody-coated SA-MTP multiwell plates and incubated for 1 hour at room temperature. After washing, wells were incubated with digoxigenylated anti-PGLALA Fc region antibody or anti-AAA Fc region antibody, respectively. After washing, the bound digoxigenylated anti-human kappa antibody complexes were incubated with horseradish peroxidase (HRP)-labeled anti-digoxigenin antibody. After another washing step, the ABTS solution was added to the wells. The color reaction product was measured by an Elisa microplate reader at a wavelength of 405 nm (reference wavelength 490...
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