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Monoclonal antibodies against human chondrocytes
In Vitro Cellular & Developmental Biology - Animal, 1996Cell-specific antigens are mainly found in cells or membrane surfaces rather than in the surrounding matrix. However, until now it was not possible to produce antibodies specific for cellular structures of chondrocytes. In 1989, Lance (Immunol. Lett.
Bujia, J.+6 more
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Humanization of Monoclonal Antibodies
1994Antibodies of predefined specificity have many potential uses in human therapy and diagnosis, and hybridoma technology (Koehler and Milstein 1975) has made possible the generation of virtually limitless amounts of such antibodies. Unfortunately, hybridoma proteins are more easily obtained from nonhuman, usually rodent, sources and the use of those ...
G. E. Mark, E. A. Padlan
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Monoclonal antibodies and therapy of human cancers
Biotechnology Advances, 2000This survey is an overview of the applications of murine, humanized and recombinant monoclonal antibodies for in vivo diagnostic and therapeutic applications. Monoclonal antibodies (mAb) have been applied to the diagnosis and therapy of an array of human diseases.
FUNARO, Ada+5 more
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An inhibitory monoclonal antibody to human acetylcholinesterases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987The monoclonal antibody AE-2 raised against acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) from human erythrocytes is shown to inhibit the enzyme activity. The reaction of the antibody with a structural epitope is investigated further. The epitope resides on monomeric, dimeric and tetrameric species of the enzyme.
Sorensen, K+3 more
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A Human Monoclonal Antibody to rh^G
Vox Sanguinis, 1986Abstract. Hybridomas secreting a human monoclonal IgG1 antibody against a variant of the rhG antigen were produced from B lymphocytes of an Rh‐negative donor with serum antibodies to D and C antigens. The antibody reacts by indirect hemagglutination with nearly all C‐ or D‐positive cells, confirming the strong association in the expression of G with D
Susan Perkins+4 more
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Humanization and Simultaneous Optimization of Monoclonal Antibody
2013Antibody humanization is an essential technology for reducing the potential risk of immunogenicity associated with animal-derived antibodies and has been applied to a majority of the therapeutic antibodies on the market. For developing an antibody molecule as a pharmaceutical at the current biotechnology level, however, other properties also have to be
Hiroyuki Tsunoda+3 more
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Human monoclonal macroglobulins with antibody activity
Seminars in Oncology, 2003Assays for specific antigen-binding activity were performed on sera from 172 patients with monoclonal macroglobulinemia defined by immunofixation electrophoresis. The sera were collected between 1970 and 2002. Mean IgM level was 1,409 mg/dL with a range from 70 to 6,800.
Alan Pestronk+5 more
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A Monoclonal Antibody for Immunopurification of Human Renin
Clinical Science, 19811. A mouse hybridoma secreting an antibody directed against human renin was obtained by fusion of spleen cells with NS 1 myeloma cells. This monoclonal antibody recognizes human and monkey renins but neither hog nor mouse renins nor the acid proteinase cathepsin D. 2. Monoclonal antibody was coupled to Sepharose 4 B.
Bernard Pau+6 more
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Human Hybridomas and Monoclonal Antibodies
1985In this review I will cover, from a cell biologist’s perspective, the biology of cell fusion and how the information derived from the field may be applicable to the production of human monoclonal antibodies. I will describe the development of the hybridoma technology, the advantages and disadvantages of making and using monoclonal antibodies, the ...
Edgar G. Engleman+3 more
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Human Monoclonal Antibodies: Recent Achievements
Hospital Practice, 1994The latest developments include an anti-HIV antibody that has 1,000 times the affinity of natural antibody and that neutralizes primary clinical isolates, and an anti-RSV antibody that reduces viral titers in mice by 12,000-fold within 24 hours.
C F Barbas rd, Dennis R. Burton
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