To search for possible ligands of CD2 distinct from CD58 (lymphocyte function-associated antigen 3), we have produced a soluble pentameric CD2-immunoglobulin (Ig) fusion protein (spCD2) linking the 182-amino acid human CD2 extracellular segment with CH2-CH3-CH4 domains of human IgM heavy chain, thus enhancing the micromolar affinity of the CD2 monomer through multimeric interaction. Using quant...

A fter the demonstration almost 20 years ago that anti-bodies to CD2 are potent inhibitors of T cell function, this cell surface glycoprotein became one of the most intensively studied of all T cell antigens (1–3). The subsequent identification of LFA-3 (CD58) as a ligand for human CD2 led to the demonstration in cell culture experiments that the CD2–CD58 interaction dramatically enhanced T cel...

Zeolitic Imidazole Framework-8 (ZIF-8) has been synthesized by dissolving Zn(NO3)2.4H2O and 2-MeIM into a methanol solvent solvothermal method. The ZIF-8 will be applied as cadmium (Cd) adsorbent in Polluted water. Several characterization methods were conducted, including XRD, FTIR, AAS. XRD analysis shows that the prominent characteristic peaks of at an angle 2θ = 7,25o; 10,26o; 12,57o; 16,22...

In a neutral aqueous environment, a new ratiometric Cd2+ fluorescent sensor 1a can successfully discriminate Cd2+ from Zn2+ by undergoing two different internal charge transfer (ICT) processes, and the high selectivity of sensor 1a to Cd2+ over some other metals was also observed. Moreover, through structure derivation and a series of NMR studies, the unique role of the 2-picolyl group (the par...

When stimulated for a few days with the mitogenic GT2 + T11(1) CD2 mAb pair and IL-2, resting T cells were induced to proliferate but the introduction into the cultures of a third CD2 mAb resulted in apoptotic cell death of 40 to 60% of the cells. The death signal was active on T cells entered the cell cycle without causing an apparent cell cycle block and without discriminating between the G1 ...

Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor complex. In vitro binding assays indicate an interaction between second cytosolic domain (CD2) of Na/K-ATPase α1 subunit and Src SH2 domain. Since SH2 domain targets Src to specific signaling complexes, we expressed CD2 as a cytosolic protein and studied whether it could act as a Src SH2 ligand in ...