Abstract
A human monoclonal rheumatoid factor (IgM, λ) produced in vitro by Epstein-Barr virus (EBV) immortalized cell line was purified from cell culture medium. Purification, based on the binding of this antibody to protein A, was carried out by adsorption on protein A-Sepharose and elution with low pH buffer. The eluted preparation (×400 purified) was radiolabeled. The specific binding of the purified rheumatoid factor (RF) to immune complexes was kept intact. This unique human monoclonal antibody is applied as a universal reagent to detect low titers of antibodies directed toward cellular antigens.
Original language | English |
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Pages (from-to) | 205-214 |
Number of pages | 10 |
Journal | Cellular Immunology |
Volume | 69 |
Issue number | 2 |
DOIs | |
State | Published - 15 May 1982 |
Externally published | Yes |