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Summary  The characterization of the architecture, structure and extracellular interactions of the  CD 6 glycoprotein, a transmembrane receptor expressed in medullary thymocytes and all mature T‐cell populations, has been enhanced by the existence of monoclonal antibodies ( mA bs) that specifically recognize the various scavenger receptor cysteine‐rich ( SRCR ) domains of the ectodomain. Using engineered isoforms of  CD 6 including or excluding each of the three  SRCR  domains, either expressed at the membranes of cells or in soluble forms, we provide conclusive and definitive evidence that domain 2 of  CD 6, previously not identifiable, can be recognized by the  CD 6  mA bs  OX 125 and  OX 126, and that  OX 124 targets domain 3 and can block the interaction at the cell surface of  CD 6 with its major ligand  CD 166. Alternative splicing‐dependent  CD 6 isoforms can now be confidently identified. We confirm that following T‐cell activation there is a partial replacement of full‐length  CD 6 by the  CD 6Δd3 isoform, which lacks the  CD 166‐binding domain, and we find no evidence for the expression of other  CD 6 isoforms at the  mRNA  or protein levels.

Domain‐specific CD 6 monoclonal antibodies identify CD 6 isoforms generated by alternative‐splicing