High-level production of a humanized immunoRNase fusion protein from stably transfected myeloma cells.
ImmunoRNases represent a highly attractive alternative to conventional immunotoxins for cancer therapy. Quantitative production of immunoRNases in appropriate expression systems, however, remains a major challenge for further clinical development of these novel compounds. Here we describe a method for high-level production and purification of a fully functional immunoRNase fusion protein from supernatants of stably transfected mammalian cells.
Krauss
Jürgen
J
National Center for Tumor Diseases, University of Heidelberg, Heidelberg, Germany.
Exner
Evelyn
E
Mavratzas
Athanasios
A
Seeber
Siegfried
S
Arndt
Michaela A E
MA
D000818:Animals; D016923:Cell Death / Q000187:drug effects; D045744:Cell Line, Tumor; D002999:Clone Cells; D004354:Drug Screening Assays, Antitumor; D005434:Flow Cytometry; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D007135:Immunoglobulin Variable Region / Q000276:immunology; D051379:Mice; D008967:Molecular Biology / Q000379:methods*; D009101:Multiple Myeloma / Q000473:pathology*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000276:immunology* / Q000494:pharmacology; D012259:Ribonuclease, Pancreatic / Q000096:biosynthesis* / Q000276:immunology* / Q000494:pharmacology; D051918:Sialic Acid Binding Ig-like Lectin 2 / Q000276:immunology; D014162:Transfection
D007135:Immunoglobulin Variable Region; D011993:Recombinant Fusion Proteins; D051918:Sialic Acid Binding Ig-like Lectin 2; C046366:angiogenin; D012259:Ribonuclease, Pancreatic