A monoclonal antibody against erythrocyte spectrin reacts with both alpha- and beta-subunits and detects spectrin-like molecules in non-erythroid cells.
A panel of nine monoclonal antibodies against the characteristic erythrocyte membrane protein spectrin has been isolated. One antibody reacts with both the 240 000 and 220 000 D alpha- and beta-subunits of spectrin after denaturation. The same antibody reacts with a 240 000 D protein present in various hemopoietic and other cell lines, as well as some smaller polypeptides, as established by western blotting and immunoautoradiography. These results indicate that the alpha- and beta-subunits of spectrin, a polypeptide of 240 000, and some smaller polypeptides present in non-erythroid cell types possess a considerable region of sequence homology, but it is not yet clear just how extensively the spectrin-like molecules and other polypeptides are related.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002460:Cell Line; D000939:Epitopes; D004912:Erythrocytes / Q000032:analysis; D005347:Fibroblasts / Q000032:analysis*; D006412:Hematopoietic Stem Cells / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D051379:Mice; D013049:Spectrin / Q000032:analysis* / Q000276:immunology; D013601:T-Lymphocytes / Q000032:analysis*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D008565:Membrane Proteins; D013049:Spectrin