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Antibody anti-streptavidin

Fig. 12. Noncompetitive hapten immunoassay procedures (A and B) using a combination of the a-type and j6-type anti-idiotype antibodies, each recognizing the framework and paratope of the anti-hapten antibody. Anti-hap, anti-hapten antibody (primary antibody) a-Id, a-type anti-idiotype antibody /J-Id, /i-type anti-idiotype antibody S, signal-generating group B, biotin SA, streptavidin. Fig. 12. Noncompetitive hapten immunoassay procedures (A and B) using a combination of the a-type and j6-type anti-idiotype antibodies, each recognizing the framework and paratope of the anti-hapten antibody. Anti-hap, anti-hapten antibody (primary antibody) a-Id, a-type anti-idiotype antibody /J-Id, /i-type anti-idiotype antibody S, signal-generating group B, biotin SA, streptavidin.
In protein microarrays, capture molecules need to be immobilized in a functional state on a solid support. In principle, the format of the assay system does not limit the choice of appropriate surface chemistry. The same immobilization procedure can be applied for both planar and bead-based systems. Proteins can be immobilized on various surfaces (Fig. 1) (12). Two-dimensional polystyrene, polylysine, aminosilane, or aldehyde, epoxy- or thiol group-coated surfaces can be used to immobilize proteins via noncovalent or covalent attachment (13,14). Three-dimensional supports like nitrocellulose or hydrogel-coated surfaces enable the immobilization of the proteins in a network structure. Larger quantities of proteins can be immobilized and kept in a functional state. Affinity binding reagents such as protein A, G, and L can be used to immobilize antibodies (15), streptavidin is used for biotinylated proteins (16), chelate for His-tagged proteins (17, 18), anti-GST antibodies for GST fusion proteins (19), and oligonucleotides for cDNA or mRNA-protein hybrids (20). [Pg.201]

Streptavidin (SA, Invitrogen, CA). antistreptavidin antibody (anti-SA, Vector). [Pg.229]

Fig. 1. Various schematics of bead display for molecular assemblies on beads. The Py subunits of the G protein (circles labeled with [i and y) are fused with either FLAG or hexahistidine tag, which recognizes the biotinylated M2 anti-FLAG antibodies on streptavidin-coated beads or chelated nickel on the dextran-treated beads. A socket and plug connecter is utilized to depict the very high-affinity interaction of the epitope tag. This modular setup allows for either a subunit (for capturing FPR-GFP) or as subunit (for capturing / 2AR-GFP) to be coupled with the fly subunit to form the complete G protein coating the bead. Fluorescent components such as GFP or ligand are indicated in green. See text for details. Fig. 1. Various schematics of bead display for molecular assemblies on beads. The Py subunits of the G protein (circles labeled with [i and y) are fused with either FLAG or hexahistidine tag, which recognizes the biotinylated M2 anti-FLAG antibodies on streptavidin-coated beads or chelated nickel on the dextran-treated beads. A socket and plug connecter is utilized to depict the very high-affinity interaction of the epitope tag. This modular setup allows for either a subunit (for capturing FPR-GFP) or as subunit (for capturing / 2AR-GFP) to be coupled with the fly subunit to form the complete G protein coating the bead. Fluorescent components such as GFP or ligand are indicated in green. See text for details.
A resistive pulse method of particle sizing was used to detect antibody-antigen binding events at a pore fabricated on a PDMS chip. The pore was typically 7-9 pm long and 1 pm in diameter. Mouse monoclonal anti-streptavidin antibody (0.75-10 pg/mL) was supposed to bind to the surface of latex colloidal particles coated with streptavidin (the antigen). This binding, which caused an increase of 1-9 nm of the particle diameter, was measured by the resistive pulse method [1031],... [Pg.349]

Figure 1. Current Nanoscale Optofluidic Sensor Arrays, (a) 3D rendering of the NOSA device, (b) 3D rendering after association of the corresponding antibody to the antigen immobilized resonator, (c) Experimental data illustrating the successful detection of 45 pg/ml of anti-streptavidin antibody. The blue trace shows the initial baseline spectrum corresponding to Fig. la where the first resonator is immobilized with streptavidin. The red trace shows the test spectra after the association of anti-streptavidin. (d) Finite difference time domain (FDTD) simulation of the steady state electric field distribution within the 1-D photonic crystal resonator at the resonant wavelength, (e) SEM image demonstrating the two-dimensional multiplexing capability of the NOSA architecture. Figure 1. Current Nanoscale Optofluidic Sensor Arrays, (a) 3D rendering of the NOSA device, (b) 3D rendering after association of the corresponding antibody to the antigen immobilized resonator, (c) Experimental data illustrating the successful detection of 45 pg/ml of anti-streptavidin antibody. The blue trace shows the initial baseline spectrum corresponding to Fig. la where the first resonator is immobilized with streptavidin. The red trace shows the test spectra after the association of anti-streptavidin. (d) Finite difference time domain (FDTD) simulation of the steady state electric field distribution within the 1-D photonic crystal resonator at the resonant wavelength, (e) SEM image demonstrating the two-dimensional multiplexing capability of the NOSA architecture.
Figure 5. Measurement of binding kinetics. Trace of recorded power at a fixed wavelength Xia as a function of time during the association of 45 pg/ml of anti-streptavidin antibody to a streptavidin functionalized resonator which clearly shows the reaction proceeding to saturation. The inset shows the correspondence of points at the start and end of the trace to the initial baseline and final red-shifted resonant spectrum. Figure 5. Measurement of binding kinetics. Trace of recorded power at a fixed wavelength Xia as a function of time during the association of 45 pg/ml of anti-streptavidin antibody to a streptavidin functionalized resonator which clearly shows the reaction proceeding to saturation. The inset shows the correspondence of points at the start and end of the trace to the initial baseline and final red-shifted resonant spectrum.
Human anti-mouse antibody (HAMA) 7, 1109 Human anti-streptavidin antibody (HASA) 513 Human antithrombin... [Pg.1860]

Biotinylated anti-streptavidin goat antibody (Vector Laboratories, Burlingame,... [Pg.113]

It is possible to perform an enzyme-linked immunosorbent assay (ELISA) using a streptavidin-coated 96-well plate the primary antibody, biotinylated-rabbit-anti-streptavidin, specifically recognizes the avidin linked to the helicate as the bioprobe. The detection limit is better than that with commercially available organic dyes such as antistreptavidin-FICT (FiB3). [Pg.555]

Fig. 34 Functionalisation of bait peptides. I Gold-labelled streptavidin is attached directly. 2 Biotin-labelled anti-FLAG antibody is bound to the FLAG on the peptide (reaction b) and this is used to attach gold-labelled streptavidin (reaction d). Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society... Fig. 34 Functionalisation of bait peptides. I Gold-labelled streptavidin is attached directly. 2 Biotin-labelled anti-FLAG antibody is bound to the FLAG on the peptide (reaction b) and this is used to attach gold-labelled streptavidin (reaction d). Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society...
Figure 8 Chemiluminescent (A and B) and bioluminescent (C) detections for immobilized hybridizations of PCR product. Dg, digoxigenin Bt, biotin Ad, avidin. Procedure A [30] Biotin moiety is incorporated into PCR products during the amplification reaction, using one 5 -biotinylated primer. The product is hybridized with a Dg-labeled probe and is immobilized on streptavidin-coated magnetic beads. This capture reaction is carried out for 30 min at 37°C. A permanent magnet is used to sediment the beads during washing to remove unbound DNA. By incubation with the washed beads for 45 min at 37°C, anti-Dg antibody conjugated to HRP enzyme is bound to the Dg-labeled probe, and luminol reaction is performed for CL detection. Procedure B [31] Wells of apolystyrene microtiter plate are activated with l-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, and then coated with a labeled cDNA probe complementary to an internal region of the target DNA. Figure 8 Chemiluminescent (A and B) and bioluminescent (C) detections for immobilized hybridizations of PCR product. Dg, digoxigenin Bt, biotin Ad, avidin. Procedure A [30] Biotin moiety is incorporated into PCR products during the amplification reaction, using one 5 -biotinylated primer. The product is hybridized with a Dg-labeled probe and is immobilized on streptavidin-coated magnetic beads. This capture reaction is carried out for 30 min at 37°C. A permanent magnet is used to sediment the beads during washing to remove unbound DNA. By incubation with the washed beads for 45 min at 37°C, anti-Dg antibody conjugated to HRP enzyme is bound to the Dg-labeled probe, and luminol reaction is performed for CL detection. Procedure B [31] Wells of apolystyrene microtiter plate are activated with l-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, and then coated with a labeled cDNA probe complementary to an internal region of the target DNA.

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See also in sourсe #XX -- [ Pg.349 ]




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