The antibody reacts with Mr 135 000 PECAM-1 polypeptide from leukocytes and endothelial cells. Detects all endothelial cells in breast. Shows erythroid differentiation in human leukemic cells.
Immunogen
Monoclonal antibody to PECAM-1 is derived from the hybridoma produced by fusion between myeloma cells and Balb/c spleen cells. Ulex Europaeus-agglutinin-I reactive glycoproteins from cultured human umbilical vein endothelial cells isolated by lecitin-affinity chromatography were used as immunogen
PECAM-1 (CE6) monoclonal antibody against PECAM-1 was produced to characterize human leukemic cells. PECAM-1 is typically an antigen that is shared by both endothelial and distinct hematopoietic cells. It is widely expressed among leukocytes and functions as cell adhesion molecule for these cells. PECAM-1 reactivity can be interpreted as a further evidence for megakaryocytic nature of distinct cell lines has been shown. However, a new useful application for this monoclonal antibody appears to be its very high reactivity against human endothelial cells. A recent review article states that in contrast to other applied endothelial markers, for instance PAL-E monoclonal antibody to endothelial cells and antibodies to factor VIII-related antigen, CE6 monoclonal antibody, reacts with all endothelial cells in human breast.