Abstract
Antigen recognition by αβ T lymphocytes is mediated via the multisubunit T-cell receptor (TCR) complex consisting of invariant CD3-γ,δ,ε, and ζ chains associated with clonotypic TCRα,β molecules. In the current report, we evaluated the molecular basis for recognition of murine TCRα proteins by H28-710 monoclonal antibody (MAb), specific for the constant region of murine TCRα chains. H28-710 is widely used in the study of the TCR complex as it is the only reagent currently available that recognizes all murine TCRα proteins, regardless of their clonotype. These data show that H28-710 is useful for the immunoprecipitation of TCRα proteins not associated with CD3 subunits, and that H28-710 effectively recognizes denatured TCRα proteins synthesized in several different cell types. Most importantly, these results demonstrate that H28 binding involves a serine/threonine-rich region between amino acids 150-177 on murine TCRα polypeptides.
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