A monoclonal antibody recognising an epitope associated with pig interleukin-2 receptors.
A monoclonal antibody is described which recognises an epitope associated with a receptor for interleukin-2 (IL-2) on pig lymphocytes. The monoclonal antibody inhibits high affinity binding of radiolabelled recombinant human IL-2 (rhIL-2) by pig lymphoblasts and also non-competitively inhibits both pig-TCGF and rhIL-2 maintained proliferation. By flow cytometry the antigen is apparently not present on freshly isolated blood lymphocytes but is detectable on small cells between 6 and 12 h after activation and on large cells by 24-h. These findings are comparable with those obtained using monoclonal antibodies recognising the 55 kDa alpha chain of the human and mouse IL-2 receptor (p55, TAC) expressed on activated cells in vivo and in vitro. However, the molecular weight of the porcine antigen is between 65 and 70 kDa.
Bailey
M
M
Department of Veterinary Medicine, University of Bristol, UK.
Stevens
K
K
Bland
P W
PW
Stokes
C R
CR
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001667:Binding, Competitive; D000939:Epitopes / Q000032:analysis*; D007376:Interleukin-2 / Q000494:pharmacology; D008213:Lymphocyte Activation; D008970:Molecular Weight; D015375:Receptors, Interleukin-2 / Q000032:analysis / Q000276:immunology*; D011994:Recombinant Proteins / Q000494:pharmacology; D013552:Swine
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007376:Interleukin-2; D015375:Receptors, Interleukin-2; D011994:Recombinant Proteins