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The monoclonal antibodies, L13/64 and RCN1/21, raised against rabbit leucocytes, have been shown, by sequential immunoprecipitation and immunoblotting, to react with the rabbit CD18 molecule. They recognise not only surface-expressed CD18 but also an intracellular form which appears to be partially glycosylated. The expression of the CD11 and CD18 glycoproteins on a wide variety of rabbit leucocyte populations has been investigated by flow cytometry, using these two monoclonal antibodies (Mabs), together with others which recognise human CD11 and CD18 proteins but cross-react with rabbit tissues. The distribution of these leucocyte integrin molecules has been shown to be similar to that observed in humans and determination of the N-terminal sequence of rabbit CD11b shows strong homology with human and mouse sequences. Of four anti-rabbit CD18 Mabs tested, only one, L13/64, has been shown to be capable of inhibiting the adhesion of fMLP-stimulated neutrophils to gelatin coated plastic and the homotypic aggregation of PMA-stimulated T cells, both of which assays have been shown to be CD18-dependent. RCN1/21 causes aggregation of unstimulated neutrophils, but it is not known whether this is due to cellular activation or agglutination.

Original publication




Journal article


Mol immunol

Publication Date





529 - 537


Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antigens, CD, CD11 Antigens, CD18 Antigens, Cell Adhesion, Cross Reactions, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Humans, Immunoblotting, Leukocytes, Macrophages, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Monocytes, Neutrophils, Precipitin Tests, Rabbits, Receptors, Leukocyte-Adhesion, Sequence Homology, Amino Acid, Spleen, Thymus Gland