| Literature DB >> 1381406 |
M Bailey1, K Stevens, P W Bland, C R Stokes.
Abstract
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.Entities:
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Year: 1992 PMID： 1381406 DOI： 10.1016/0022-1759(92)90309-h
Source DB: PubMed Journal: J Immunol Methods ISSN： 0022-1759 Impact factor: 2.303