A monoclonal antibody to the α2 integrin subunit cross-reacts with RGD-dependent epitopes in fibrinogen
作者： MARTINE JASPERS , SYLVIE VEKEMANS , GEERT CARMELIET , FRED van LEUVEN , BART de STROOPER
关键词: Monoclonal 、 Molecular biology 、 Antigen 、 Monoclonal antibody 、 Fibronectin 、 Epitope 、 Antibody 、 Platelet membrane glycoprotein 、 Affinity chromatography 、 Biology
摘要: Monoclonal antibodies were raised against platelet integrins purified by affinity chromatography. Two monoclonal (5C5 and 3H8) reacted with the alpha 2 subunit of VLA-2 in Western blotting. The antibody 3H8 also fibrinogen blots ELISA tests. CNBr fragmentation chain generated two peptides which still recognized this N-terminus sequencing these fragments showed that they non-overlapping alpha-chain as only common epitope an RGD(F)/RGD(S) sequence. Dot tests recognized, however lower affinity, fibronectin collagen IV, are RGDS containing extracellular matrix proteins. assumption Mab recognizes RGD sequence, was further supported findings binding to partially inhibited RGDF able inhibit aggregation.
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