Report of the key comparison CCQM-K88 : determination of lead in lead-free solder containing silver and copper

The CCQM-K88 key comparison was organised by the Inorganic Analysis Working Group of CCQM to test the abilities of the national metrology institutes to measure the mass fraction of lead in lead-free solder containing silver and copper. National Metrology Institute of Japan (NMIJ), National Institute of Metrology P. R. China (NIM) and Korea Research Institute of Standards and Science (KRISS) acted as the coordinating laboratories. The participants used different measurement methods, though most of them used inductively coupled plasma optical emission spectrometry (ICP-OES) or isotope-dilution inductively coupled plasma mass spectrometry (ID-ICP-MS). Accounting for relative expanded uncertainty, comparability of measurement results was successfully demonstrated by the participating NMIs for the measurement of the mass fraction of lead in lead-free solder at the level of 200 mg/kg. It is expected that metals at mass fractions greater than approximately100 mg/kg in lead-free solder containing silver and copper can be determined by each participant using the same technique(s) employed for this key comparison to achieve similar uncertainties mentioned in the present report.Fil: Hioki, Akiharu. National Metrology Institute of Japan (NMIJ); JapónFil: Nonose, Naoko. National Metrology Institute of Japan (NMIJ); JapónFil: Liandi, Ma. National Institute of Metrology (NIM); ChinaFil: Jingbo, Chao. National Institute of Metrology (NIM); ChinaFil: Liuxing, Feng. National Institute of Metrology (NIM); ChinaFil: Chao, Wei. National Institute of Metrology (NIM); ChinaFil: Cho, Kyung Haeng. Korea Research Institute of Standards and Science (KRISS); Corea del SurFil: Suh, Jung Ki. Korea Research Institute of Standards and Science (KRISS); Corea del SurFil: Min, Hyung Sik. Korea Research Institute of Standards and Science (KRISS); Corea del SurFil: Lim, Youngran. Korea Research Institute of Standards and Science (KRISS); Corea del SurFil: Recknagel, Sebastian. Federal Institute for Materials Research and Testing (BAM); AlemaniaFil: Koenig, Maren. Federal Institute for Materials Research and Testing (BAM); AlemaniaFil: Vogl, Jochen. Federal Institute for Materials Research and Testing (BAM); AlemaniaFil: Caciano de Sena, Rodrigo. Instituto Nacional de Metrologia, Qualidade e Tecnologia (INMetro); BrasilFil: dos Reis, Lindomar Augusto. Instituto Nacional de Metrologia, Qualidade e Tecnologia (INMetro); BrasilFil: Borinsky, Mónica. Instituto Nacional de Tecnología Industrial (INTI); ArgentinaFil: Puelles, Mabel. Instituto Nacional de Tecnología Industrial (INTI); ArgentinaFil: Hatamleh, Nadia. Instituto Nacional de Tecnología Industrial (INTI); ArgentinaFil: Acosta, Osvaldo. Instituto Nacional de Tecnología Industrial (INTI); ArgentinaFil: Turk, Gregory. National Institute of Standards and Technology (NIST); Estados UnidosFil: Rabb, Savelas. National Institute of Standards and Technology (NIST); Estados UnidosFil: Sturgeon, Ralph. National Research Council (NRC); CanadáFil: Methven, Brad. National Research Council (NRC); CanadáFil: Rienitz, Olaf. Physikalisch-Technische Bundesanstalt (PTB); AlemaniaFil: Jaehrling, Reinhard. Physikalisch-Technische Bundesanstalt (PTB); AlemaniaFil: Konopelko, L. A. D. I. Mendeleev Institute for Metrology (VNIIM); RusiaFil: Kustikov, Yu. A. D. I. Mendeleev Institute for Metrology (VNIIM); RusiaFil: Kozyreva, S. B. D. I. Mendeleev Institute for Metrology (VNIIM); RusiaFil: Korzh, A. A. D. I. Mendeleev Institute for Metrology (VNIIM); Rusi

Improved mean positions and proper motions for the 995 FK4 sup stars not included in the FK5 extension

SIGLEAvailable from TIB Hannover / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekDEGerman

Characterization and screening of IgG binding to the neonatal Fc receptor

The neonatal Fc receptor (FcRn) protects immunoglobulin G (IgG) from degradation and increases the serum half-life of IgG, thereby contributing to a higher concentration of IgG in the serum. Because altered FcRn binding may result in a reduced or prolonged half-life of IgG molecules, it is advisable to characterize Fc receptor binding of therapeutic antibody lead candidates prior to the start of pre-clinical and clinical studies. In this study, we characterized the interactions between FcRn of different species (human, cynomolgus monkey, mouse and rat) and nine IgG molecules from different species and isotypes with common variable heavy (VH) and variable light chain (VL) domains. Binding was analyzed at acidic and neutral pH using surface plasmon resonance (SPR) and biolayer interferometry (BLI). Furthermore, we transferred the well-accepted, but low throughput SPR-based method for FcRn binding characterization to the BLI-based Octet platform to enable a higher sample throughput allowing the characterization of FcRn binding already during early drug discovery phase. We showed that the BLI-based approach is fit-for-purpose and capable of discriminating between IgG molecules with significant differences in FcRn binding affinities. Using this high-throughput approach we investigated FcRn binding of 36 IgG molecules that represented all VH/VL region combinations available in the fully human, recombinant antibody library Ylanthia. Our results clearly showed normal FcRn binding profiles for all samples. Hence, the variations among the framework parts, complementarity-determining region (CDR) 1 and CDR2 of the fragment antigen binding (Fab) domain did not significantly change FcRn binding. 2014 Landes Bioscienc

Prdm6 Is Essential for Cardiovascular Development In Vivo

Prdm6 Is Essential for Cardiovascular Development In Viv