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Monoclonal Antibodies Specific for Variable and Constant Domains of Murine λ Chains
Author(s) -
BOGEN B.
Publication year - 1989
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1989.tb01125.x
Subject(s) - antibody , monoclonal antibody , microbiology and biotechnology , chemistry , immunofluorescence , fluorescein isothiocyanate , biotinylation , radioimmunoassay , immunoglobulin g , immunoglobulin light chain , epitope , biochemistry , biology , immunology , fluorescence , physics , quantum mechanics
Rat monoclonal antibodies directed against the BALB/c myeloma protein M315 (α,λ2) are described. 9A8 (IgG1) binds the V domain of λ2 and cross‐reacts with λ1 and λ3 chains. 2B6 (IgG2a) is directed to the C domain of λ2 and cross‐reacts λ3. The antibodies bind isolated chains as well us complete immunoglobulins. The monoclonals detect soluble immunoglobulin (radioimmunoassay), immunoglobulin immobilized on polystyrene (enzyme‐linked immunosorbent assay), immunoglobulin bound to nitrocellulose (immunoblotting), and surface immunoglobulin intercalated in cell membranes (immunofluorescence). The antibodies are easily purified on protein G immunosorbents and may be biotinylated or conjugated with fluorescein isothiocyanate without loss of capacity to bind. In addition to the anti‐λ antibodies, a C α 2/C α 3‐specific monoclonal antibody, 8D2 (IgG2a) is described.