A monoclonal antibody D51 recognizes the transferrin-receptor structure.
A monoclonal antibody D51 has been obtained during immunization against human fetal thymus. The antibody binds to a variety of leukemic cells. This is similar to the staining pattern of the mAb OKT9 and L 5.1, which recognize the transferrin receptor. However, there are some differences. The antibody immunoprecipitates a protein present on Molt-4 cells. Under reducing conditions this protein has a molecular weight of 90 K dalton. Under non-reducing conditions it has a molecular weight of 180 K dalton. This suggests a dimeric structure. The consecutive immunoprecipitation with D51 and OKT9, respectively, demonstrates that both antibodies recognize the structure of the transferrin receptor.
Gross
H J
HJ
D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D000951:Antigens, Neoplasm / Q000032:analysis; D006801:Humans; D007938:Leukemia / Q000276:immunology; D008214:Lymphocytes / Q000276:immunology; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000276:immunology* / Q000378:metabolism; D011990:Receptors, Transferrin; D014168:Transferrin / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin