Most tumor-associated antigens represent self-proteins and as a result are poorly immunogenic due to immune tolerance. Here we show that tolerance to carcinoembryonic antigen (CEA), which is overexpressed by the majority of lethal malignancies, can be reversed by immunization with a CEA-derived peptide. This peptide was altered to make it a more potent T cell antigen and loaded onto dendritic cells (

We report on an improved measurement of the 2νββ half-life of 136 Xe performed by EXO-200. The use of a large and homogeneous time projection chamber allows for the precise estimate of the fiducial mass used for the measurement, resulting in a small systematic uncertainty. We also discuss in detail the data analysis methods used for double-beta decay searches with EXO-200, while emphasizing those directly related to the present measurement. The 136 Xe 2νββ half-life is found to be T 2νββ 1/2 = 2.165 ± 0.016(stat) ± 0.059(sys) · 10 21 years. This is the most precisely measured half-life of any 2νββ decay to date.

is an experiment designed to search for double beta decay of 136 Xe with a single-phase, liquid xenon detector. It uses an active mass of 110 kg of xenon enriched to 80.6% in the isotope 136 in an ultra-low background time projection chamber capable of simultaneous detection of ionization and scintillation. This paper describes the EXO-200 detector with particular attention to the most innovative aspects of the design that revolve around the reduction of backgrounds, the efficient use of the expensive isotopically enriched xenon, and the optimization of the energy resolution in a relatively large volume.-1 -arXiv:1202.2192v2 [physics.ins-det]

We have developed a class of binding proteins, called avimers, to overcome the limitations of antibodies and other immunoglobulin-based therapeutic proteins. Avimers are evolved from a large family of human extracellular receptor domains by in vitro exon shuffling and phage display, generating multidomain proteins with binding and inhibitory properties. Linking multiple independent binding domains creates avidity and results in improved affinity and specificity compared with conventional single-epitope binding proteins. Other potential advantages over immunoglobulin domains include simple and efficient production of multitarget-specific molecules in Escherichia coli, improved thermostability and resistance to proteases. Avimers with sub-nM affinities were obtained against five targets. An avimer that inhibits interleukin 6 with 0.8 pM IC50 in cell-based assays is biologically active in two animal models.