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• W2948289898 abstract "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." @default.
• W2948289898 created "2019-06-14" @default.
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• W2948289898 date "2019-06-23" @default.
• W2948289898 modified "2023-10-17" @default.
• W2948289898 title "Domain‐specific <scp>CD</scp>6 monoclonal antibodies identify <scp>CD</scp>6 isoforms generated by alternative‐splicing" @default.
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• W2948289898 doi "https://doi.org/10.1111/imm.13087" @default.
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