BD Multitest™ Anti-Human CD8 FITC/CD38 PE/CD3 PerCP/HLA-DR APC

CD8, clone SK1, is derived from hybridization of mouse NS-1 myeloma cells with spleen cells from BALB/c mice immunized with human peripheral blood T lymphocytes.

CD38, clone HB7, is derived from hybridization of mouse P3-X63-Ag8.653 myeloma cells with spleen cells from BALB/c mice immunized with the BJAB cell line.

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–HLA-DR, clone L243, is derived from the hybridization of mouse NS-1/1-Ag4 myeloma cells with spleen cells from BALB/c mice immunized with the human lymphoblastoid B-cell line RPMI 8866.

CD8 recognizes an antigen expressed on the 32-kDalton (kDa) α subunit of a disulfide-linked bimolecular complex. The cytoplasmic domain of the α subunit of the CD8 antigen is associated with the protein tyrosine kinase p56^lck. The CD8 molecule interacts with class I major histocompatibility complex (MHC) molecules resulting in increased adhesion between the CD8⁺T lymphocytes and the target cells. Binding of the CD8 molecule to class I MHC molecules enhances the activation of resting T lymphocytes.

CD38 recognizes an integral membrane glycoprotein, Mr 45 kDa, with a protein core of 35 kDa.

CD3 recognizes 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 kDa. The antigen recognized by the CD3 antibody is noncovalently associated with either α/β or γ/δ TCR (70 to 90 kDa).

Anti–HLA-DR recognizes a human class II MHC antigen. The antigen is a transmembrane glycoprotein composed of α and β subunits that have molecular weights of 36 and 27 kDa, respectively. Anti–HLA-DR reacts with a nonpolymorphic HLA-DR epitope and does not cross-react with HLA-DQ or HLA-DP molecules.