Anti–TCR-α/β-1, clone WT31, is derived from hybridization of mouse Sp2/0-Ag14 myeloma cells with spleen cells from BALB/c mice immunized with human thymocytes.
Anti–TCR-γ/δ-1, clone 11F2, is derived from hybridization of mouse Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with a Sepharose® bead/CD3/γ/δ TCR complex.
CD3, clone SK7, is derived from hybridization of mouse NS-1 myeloma cells with spleen cells from BALB/c mice immunized with human thymocytes.
Anti–TCR-α/β-1 recognizes a conformational epitope formed by the T-cell receptor (TCR) for antigen and the CD3 epsilon chain. The α/β TCR is a disulﬁde-linked 80-kilodalton (kd) heterodimer consisting of a 44-kd α chain and a 37-kd β chain.
Anti–TCR-γ/δ-1 reacts with a framework epitope of the γ/δ T-cell antigen receptor (TCR). The γ/δ TCR is a heterodimeric glycoprotein that is noncovalently associated with the CD3 antigen. The γ and δ TCR chains are composed of constant and variable regions, each encoded by distinct gene segments. The γ chain forms either disulﬁde-linked or non–disulﬁde-linked heterodimers with the δ subunit.
CD3 reacts with the epsilon chain of the CD3 antigen/T-cell antigen receptor (TCR) complex. This complex is composed of at least six proteins that range in molecular weight from 20 to 30 kd. The antigen recognized by CD3 antibodies is noncovalently associated with either α/β or γ/δ TCR (70 to 90 kd).