Analysis of HLDA9 mAbs on plasmacytoid dendritic cells.
Authors: Cabezon R, Sintes J, Llinas L, Benitez-Ribas D
Immunol. Lett., 2011;134(2):167-73.
Species: Human
Sample Type: Whole Cells
Application: Flow
New B-cell CD molecules.
Authors: Matesanz-Isabel J, Sintes J, Llinas L, de Salort J, Lazaro A, Engel P
Immunol. Lett., 2011;134(2):104-12.
Species: Human
Sample Type: Whole Cells
Application: Flow
Impaired Epstein-Barr virus-specific CD8+ T-cell function in X-linked lymphoproliferative disease is restricted to SLAM family-positive B-cell targets.
Authors: Hislop AD, Palendira U, Leese AM
Blood, 2010;116(17):3249-57.
Species: Human
Sample Type: Whole Cells
Application: Flow
Human T-cell leukemia virus type 1 (HTLV-1) p12I down-modulates ICAM-1 and -2 and reduces adherence of natural killer cells, thereby protecting HTLV-1-infected primary CD4+ T cells from autologous natural killer cell-mediated cytotoxicity despite the reduction of major histocompatibility complex class I molecules on infected cells.
Authors: Banerjee P, Feuer G, Barker E
J. Virol., 2007;81(18):9707-17.
Species: Human
Sample Type: Whole Cells
Application: Flow

NTB-A (NK-T-B-antigen), also known as Ly108 and SLAMF6, is a 60 kDa type I transmembrane glycoprotein that belongs to the SLAM subgroup of the CD2 family (1). Mature human NTB-A contains a 205 amino acid (aa) extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain. It also contains a 21 aa transmembrane segment and an 84 aa cytoplasmic domain with two immunoreceptor tyrosine-based switch motifs (ITSMs) (2, 3). An alternately spliced isoform is truncated in the cytoplasmic domain and lacks the two ITSMs. Within the ECD, human NTB-A shares 48% aa sequence identity with mouse and rat NTB-A. The ECD of human NTB-A shares 19%‑34% aa sequence identity with comparable regions of human 2B4, BLAME, CD2F-10, CD84, CD229, CRACC, and SLAM. NTB-A is expressed on the surface of NK, T, and B lymphocytes as well as eosinophils (2, 4, 5). It interacts homophilically through weak associations between the Ig-V domains (2, 5‑7). NTB-A functions as an activating coreceptor on NK and T cells (2, 5, 6, 8). Tyrosine phosphorylation in the membrane proximal ITSM enables specific association with EAT-2, an interaction that is required for NTB-A mediated cytotoxicity of NK cells (9). Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-gamma by NK cells (5, 9). This interaction is independent of EAT-2 binding and appears to involve the membrane distal ITSM (5, 9). NTB-A deficient mice show weakened Th2 responses and elevated levels of neutrophil-derived inflammatory mediators (10). On B cells, NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity (5, 11).

1. Veillette, A. (2006) Immunol. Rev. 214:22.
2. Bottino, C. et al. (2001) J. Exp. Med. 194:235.
3. Fraser, C.C. et al. (2002) Immunogenetics 53:843.
4. Munitz, A. et al. (2005) J. Immunol. 174:110.
5. Valdez, P.A. et al. (2004) J. Biol. Chem. 279:18662.
6. Flaig, R.M. et al. (2004) J. Immunol. 172:6524.
7. Cao, E. et al. (2006) Immunity 25:559.
8. Stark, S. and C. Watzl (2006) Int. Immunol. 18:241.
9. Eissmann, P. and C. Watzl (2006) J. Immunol. 177:3170.
10. Howie, D. et al. (2005) J. Immunol. 174:5931.
11. Kumar, K.R. et al. (2006) Science 312:1665.