Abstract
CD101 is a cell surface protein with a molecular weight of about 140 kDa and seven Ig-like loops in its extra-cellular domain, that was first described in our laboratory, using two different monoclonal antibodies (mAb), BB27 and BA27 (1,2). The two anti-CD101 mAbs BB27 and BA27 were generated by immunization of BALB/c mice with the CD4+CD8+ thymic clone B12 (3). These mAbs recognize CD101, a disulfide bonded-homodimer, on subsets of circulating T lymphocytes.
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