Monoclonal antibodies availability

Table 11 lists the reactivity of antibodies to various lymphoreticular neoplasms in formalin- or B5-fixed tissues. Many of the monoclonal antibodies available to B- or T-cell lymphomas are not strictly lineage specific (MBl, MB2, LNl, MTl). CD20 (L26) (45) for B-cells and CD45RO (UCHL-1) (46) for T-cells has been shown to be fairly specific. UCHL-1 is not present on all T-cells, therefore one may want to include another T-cell marker to detect T-cell lymphomas. (3-FI (47), which recognizes a framework epitope on the T-cell P chain antigen receptor, and anti-CD3 (48) may be particularly promising in specifically detecting T-cell lymphomas. 

The mI contribution can also be determined from experiments with columns of the same size packed with immunoadsorbents of varying capacities (22). Because of the low amount of monoclonal antibody available, these experiments were performed by immobilizing various quantities of polyclonal anti-HSA antibody on the silica matrix. The results for an 83.3 mm s-1 flow rate are summarized in Table 2. An important decrease of the apparent adsorption rate constant is observed when the column capacity is increased. 

Numerous investigators have reported and reviewed the chnical application of monoclonal antibodies in various areas, including organ transplantation, neoplastic diseases, severe sepsis, and chronic inflammatory diseases. Collectively, these antibodies generally did not produce major adverse effects. The rapid development of antibodies against murine monoclonal antibodies is one of the most important clinical hmitations to their therapeutic use, but the development of humanized (chimeric human/ murine) monoclonal antibodies has improved their safety. Monoclonal antibodies have also been used in non-immune mediated diseases, such as cancer, septic shock, reperfusion, and as antiplatelet drugs. Treatment of neoplastic diseases with monoclonal antibodies is theoretically attractive. Unfortunately none of the monoclonal antibodies available at present has been demonstrated to be strictly tumor-specific, and binding of antibody to normal cells has been shown to be the major unknown factor for toxicity (6). 

Using 1° antibodies made in the different species is the easiest way to localize multiple proteins (Chapter 11). However, it is not possible to get all 1° antibodies needed from a different species. This is especially true because there are so many mouse monoclonal antibodies available. Eventually, an experiment will need two mouse 1° antibodies or two rabbit 1° antibodies. This chapter presents the concept of combining multiple 1° antibodies made in the same species of animals. Two different approaches include block-between method and labeled Fab procedure (Lewis et al., 1993) that is available as the commercial product, Zenon (Molecular Probes/Invitrogen). 

Commercially available dtugs used for therapeutic therapy comprise up to date mainly injectable monoclonal antibodies like Infliximab (Remicade ) and Adalimumab (Humira ) or TNF-receptor derivatives like Etanercept (Enbrel ) (Fig. 3). One possible way of action of these reagents is the neutralization of TNF, thereby blocking its inflammatory effects and dampening (auto)immune responses [3, 4]. 

In addition to the three types of immunological product that are generally available there are two further types synthetic peptide vaccines and monoclonal antibodies. Both have been extensively investigated but neither has, as yet, a place in conventional prophylaxis or therapeutics. 

In the dialyzed batch start-up phase and the subsequent continuous operation a substantial increase in viable cell density and monoclonal antibody (MAb) titer was observed compared to a conventional suspension culture. The raw data, profiles of the viable cell density, viability and monoclonal antibody titer during the batch start-up and the continuous operation with a dialysis flow rate of 5 L/d are shown in Figures 17.6 and 17.7. The raw data are also available in tabular form in the corresponding input file for the FORTRAN program on data smoothing for short cut methods provided with the enclosed CD. 

Generation of antibodies that can recognize and bind to specific viruses is straightforward. A sample of live or attenuated virus, or a purified component of the viral caspid, can be injected into animals to stimulate polyclonal antibody production (or to facilitate monoclonal antibody production by hybridoma technology). Harvested antibodies are then employed to develop specific immunoassays that can be used to screen test samples routinely for the presence of that specific virus. Immunoassays capable of detecting a wide range of viruses are available commercially. The sensitivity, ease, speed and relative inexpensiveness of these assays render them particularly attractive. 

There are literally hundreds of markers that are currently available for the mouse and human than can be used to characterize lymphoid and myeloid cells and subsets in primary and secondary lymphoid organs. Many of the markers expressed in mammals are highly conserved across species and have been designated as genetic clusters of differentiation (CD). CDs can be identified with fluorescently labeled monoclonal antibodies. As presented previously, when combined with other fluorescent probes, important information on intracellular biochemistry and cell function can be obtained. Many of the biochemical markers used by immunotoxicologists are common to other... 

BioPortfolio. IDEC (NASDAQ IDPH) has halted clinical trials of its therapeutic monoclonal antibody IDEC-131 [online]. Available at http //www.bioportfolio.com/news/ btech 061102 l.htm [Accessed 2006]... 

The decision regarding whether to use a polyclonal antibody or monoclonal antibody depends on a number of factors, the most important of which are its intended use and whether the antibody is readily available from commercial suppliers or researchers. The concentration and purity levels of specific antibody are higher in monoclonal antibodies. However, polyclonal antibodies are known to have a higher affinity and a better specificity than monoclonal antibodies, because they are produced by a large number of B cell clones each generating antibodies to a specific epitope, and because polyclonal sera are a composite of antibodies with unique specificities (Lipman et al. 2005). 

The protocol for double/multiple immunolabeling using haptenylated primary antibodies is essentially the same as with primary antibodies of different IgG isotypes. These protocols can be easily customized depending on the availability of primary antibodies for your research requirements. For instance, you may have at your disposal a pair of monoclonal antibodies of the same IgG isotype, and only one of them is haptenylated. In this case, you have to carry out the immunostaining in two steps in the first step you visualize the unlabeled first primary antibody with a secondary species-specific antibody, and in the second step you can detect the second primary haptenylated antibody via another secondary antibody directed against the corresponding hapten. Should the hapten be a fluorophore, it can be visualized directly in a fluorescent microscope and you do not need the second step... 

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