Monoclonal antibodies specific for the C-terminus of the laminin B2 subunit. Evidence for glycosylation differences between murine and human laminin.
We have raised a panel of monoclonal antibodies against a beta-galactosidase fusion protein (XLB2.1) containing the C-terminal 153 amino acids of the murine laminin B2 subunit. Five of the nine antibodies characterized recognize human placental laminin as well as murine Engelbreth-Holm-Swarm (EHS)-tumour laminin. Only two of the antibodies recognize both rat parietal-yolk-sac laminin and murine EHS-tumour laminin. Two antibodies recognize an epitope on the human laminin B2 subunit which is masked by N-linked oligosaccharide in murine EHS-tumour laminin. These antibodies also fail to bind to laminin from adult-mouse tissues. These results demonstrate a species-specific difference in the glycosylation of the laminin B2 subunit.
Brown
J C
JC
Research Centre, Ciba-Geigy Pharmaceuticals, Horsham, West Sussex, U.K.
Spragg
J H
JH
Taylor
P W
PW
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D015153:Blotting, Western; D006023:Glycoproteins / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D007797:Laminin / Q000276:immunology*; D051379:Mice; D011499:Protein Processing, Post-Translational; D051381:Rats; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D007797:Laminin