Production of monoclonal antibodies toward bovine interferons-alpha suitable for immunopurification.
Five murine hybridoma clones, producing monoclonal antibodies (MAbs) to bovine interferon-alpha (BoIFN-alpha) were established. One of these, F12, secreted MAbs giving high titers, in ELISA tests, neutralizing both BoIFN-alpha, -alpha C, and BoIFN-alpha D activities, belonging to the mouse IgG1 class, and having a binding affinity constant of 10(8) M-1. F12 MAbs were used for immunoaffinity purification of BoIFN-alpha, and recombinant BoIFN-alpha C from Escherichia coli extracts was purified to homogeneity in SDS-PAGE analysis and to a specific activity of 2 X 10(8) U/mg with 90% recovery of activity.
Kobiler
D
D
Department of Biochemistry, Israel Institute for Biological Research, Ness-Ziona.
Grosfeld
H
H
Leitner
M
M
Monzain
R
R
Frist
C
C
Seri
T
T
Cohen
S
S
Velan
B
B
Shafferman
A
A
Gozes
Y
Y
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis*; D002846:Chromatography, Affinity; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D006825:Hybridomas; D007118:Immunoassay; D007074:Immunoglobulin G / Q000145:classification; D007370:Interferon Type I / Q000276:immunology*; D051379:Mice; D011994:Recombinant Proteins
D000911:Antibodies, Monoclonal; D007074:Immunoglobulin G; D007370:Interferon Type I; D011994:Recombinant Proteins