Antibody schematic representation

Humanized Monoclonal Antibodies. Figure 1 Schematic representation of mouse, human, chimeric and... 

FIG. 4.1. Schematic representation of two antibodies reacting with a continuous and a discontinuous epitope of a protein antigen interacting residues are indicated in black. If the individual loops of a discontinuous epitope are able to bind to the antibody paratope on their own, they may be given the status of continuous epitope. The inset shows the three loops of an antibody VH chain which form part of the paratope... 

Fig. 1.3 Schematic representation of an antibody molecule. Adapted from http //probes. invitrogen. com/handbook/boxes/0439.html...

Fig. 2.1 Schematic representation of the procedure for generating and using primary antibody Fab fragment complexes...

Fig. 6.13. Schematic representation of a selective delivery obtained by antibody-directed en-zyme-prodrug therapy (ADEPT). An exogenous enzyme is coupled to a monoclonal antibody (mAb) targeted for tumor cells. In a second step, a prodrug is administered, which, as a selective substrate of the exogenous enzyme, will be selectively activated at the tumor site.

Fig. 5. Schematic representation of the domain structure of albumin, the position of the disulfide loops, and the fragments of the molecule that have been isolated. Included in the figure are the cleavage methods used to obtain the fragments plus the regions to which the restricted antibody populations used in these experiments are directed. Reprinted, with permission, from Teale and Benjamin (1976). Copyright by the American Society of Biological Chemists, Inc.

Figure 11.4 Schematic representation of ELISAs for the detection of IFN-a-IFN-tx and HS A-IFN-a aggregates. IFN-a-fFN-a aggregates are detected using the same monoclonal anti-fFN-a antibody (LI-1) as capture and detection antibodies. HSA-IFN-a aggregates are captured by the anti-IFN-a antibody LI-1, and IFN-a-bound HSA is identified by a polyclonal and anti-HSA antibody. For simplicity, aggregates are illustrated at a 1 1 molar ratio (HRP = horseradish peroxidase).

Figure 3.24 Schematic representation of the analytical protocol (A) Capture of the ALP-loaded CNT tags to streptavidin-modified magnetic beads by a sandwich DNA hybridization (a) or Ab-Ag-Ab interaction (b). (B) Enzymatic reaction. (C) Electrochemical detection of the product of the enzymatic reaction at the CNT-modified glassy carbon electrode MB, Magnetic beads P, DNA probe 1 T, DNA target P2, DNA probe 2 Abl, first antibody Ag, antigen Ab2, secondary...

Figure 1.1. Schematic representation of four major liposome types. Conventional liposomes are either neutral or negatively charged. Stealth liposomes are sterically stabilized and carry a polymer coating to obtain a prolonged circulation time in the body. Immunoliposomes are antibody targeted liposomes and can consist of either conventional or sterically stabilized liposomes. Positive charge on cationic liposomes can be created in various ways. Reproduced from reference [112] with permission.

Fig. 7. Schematic representation of the principle of TUNEL assay. The enzyme TdT catalyzes a template-independent addition of bromolated deoxyuridine triphosphates (Br-dUTP) to the 3 -OH ends of double- and single-stranded DNA. After Br-dUTP incorporation, DNA break sites are identified by an FITC-labeled anti-BrdU monoclonal antibody.

Fig. 3. Schematic representation of noncompetitive immunoassays. (A) Two-site immunometric assays (sandwich assays) and (B) single-antibody (single-epitope) immunometric assays.

Fig. 9. Schematic representation of the noncompetitive immunoassay of triiodothyronine using a solid-phase immobilized hapten for masking an unoccupied antibody.

Fig. 11. Schematic representation of the binding properties of anti-idiotype antibodies and antimetatype antibodies. V, hapten a-Id, a-type anti-idiotype antibody /i-Id, /i-type anti-idiotype antibody Met, anti-metatype antibody anti-C-region, antibodies recognizing the constant region of a primary antibody (recognizing isotype or allotype).

Figure 1. Schematic representations of significant biological functions displayed by host-guest complexation in homogeneous solutions or at membrane surfaces, (a) Separation (e.g., antibody-antigen complex formation), (b) Transformation (e.g., enzymatic reaction), (c) Translocation (e.g., carrier- or channel-mediated transport), (d) Transduction (e.g., receptor-mediated transmembrane signaling).

Figure 10.3. Schematic representation of monoclonal antibody production using immortalized hybrid cells that secrete antibodies selective for the target antigen. The mortal, immune B cells Isolated from mice immunized with a target antigen are fused with myeloma, immortal B cells that express defective antibodies. The selecting of antigen-specific, immortal hybrid cells (hybridomas) results in identification of unique clones of cells that express antibodies with high specificity and affinity (monoclonal antibodies). These cells are cloned and expanded for large-scale monoclonal antibody preparations.

Figure 10.4. Schematic representation of antibody distribution into extravascular space across endothelial cells lining blood capillaries and into the tumor mass. Some of these antibody molecules may be further distributed into lymphatic capillaries.

Figure 8.2. Schematic representation of a competitive enzyme-linked immunosorbent assay using (a) immobilized antigen or (b) immobilized antibody.

Fig. 1 Schematic representation of an antibody molecule (human subclass IgGi). The homologous domains within the heavy (H) and light (L) chains are indicated, and the hypervariable segments within the variable (V) regions are shown. Inter-and intra-chain disulfide bridges are depicted by solid lines...

Fig. 18.3. Schematic representation of the photoaffinity immobilization of the antibody cholera toxin (anti-CT). After irradiation of the photobiotin layered electrode in presence of the antibody, a covalent bond has been formed between the electrode and the antibody keeping its accessibility for immunoreactions with HRP-IgG anti-rabbit antibody.

Fig. 1. Schematic representation of the three distinct regions of LPS. The repating unit structure of the O-polysaccharide may be recognized by antibodies with specificities for determinants associated with the terminal non-reducing residues (antibody type 1 b) or internal sequences often spanning more than one repeating sequence (cf. Refs. [72, 73])...

Figure 11.4 Schematic representation of the multiple extraction procedure with the antibody-conjugated silica nanoparticles doped with magnetic nanoparticles (MNP) being added and extracted stepwise and the corresponding antibody-conjugated silica nanoparticles doped with fluorescent dyes (FNP) being added post-magnetic extraction of cell samples.40 (Reprinted with permission from J. E. Smith et al., Anal. Chem., 2007, 79, 3075-3082. Copyright 2007 American Chemical Society.) (See color insert.)...

Figure 32.9. Schematic representation of Type I hypersensitivity. Induction Resident respiratory tract dendritic cells (DC) take and process antigen, mature, migrate to the draining lymph nodes, and present antigen to T lymphocytes. Activated T-lymphocytes, in turn, activate B-cell differentiation into antibody-producing plasma cells. IL-4 promotes Ig isotype class switching from IgM to IgE and promotes mast cell development. IgE is associated with mast cells. Elicitation Allergen crosslinks the mast-cell-bound IgE, thereby causing the release of preformed mediators and cytokines. (See Table 32.7.) Inflammation and bronchoconstriction occur.

The MALDI mass spectrum obtained from the peptides resulting from the enzymatic digestion (Asp-N) of the bFGF protein (A) spectrum before and (B) spectrum after immunoprecipitation with an antibody directed against the recombinant protein. The peaks marked correspond to either Cu adducts or doubly charged ions. (C) Schematic representation of the observed peptides. A continuous line corresponds to a peptide that links to the antibody, and a dotted line to a peptide that does not link. Reproduced (modified) from Zhao Y.M., Muir T.W., Kent S.B.FL, Tisher E., Scardina J.M. and Chait B.T., Proc. Natl. Acad. Sci. USA, 93, 4020M024, 199, with permission. 

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