Rabbit Anti-Human BST1 (internal) Polyclonal antibody

The effect of firing temperatures on phase formation and microstructure of barium stannate titanate [Ba(Sn0.1Ti0.9)O-3-, BST10] ceramics were investigated. BST1 was synthesized via a combustion method, at various calcination and sintering temperatures. It was found that, a single perovskite of BST10 powders was obtained with a calcinations temperature of 1200 degrees C. The percent of the perovskite phase and the lattice parameter were increased with increasing calcination temperatures. The average particle size was increased front 0.48 to 1.69 mu m by increasing the calcined temperature from 600 to 1200 degrees C. The average grain sizes were increased from 0.99 to 17.77 mu m by increasing the sintering temperature from 1250 to 1450 degrees C. The maximum density and dielectric constant were observed in sintered samples at 1350 degrees C.

CD157/Bst1 is a dual-function receptor and beta-NAD+-metabolizing ectoenzyme of the ADP-ribosyl cyclase family. Expressed in human peripheral blood neutrophils and monocytes, CD157 interacts with extracellular matrix components and regulates leukocyte diapedesis via integrin-mediated signalling in inflammation. CD157 also regulates cell migration and is a marker of adverse prognosis in epithelial ovarian cancer and pleural mesothelioma. One form of CD157 is known to date: the canonical sequence of 318 aa from a 9-exon transcript encoded by BST1 on human chromosome 4. Here we describe a second BST1 transcript, consisting of 10 exons, in human neutrophils. This transcript includes an unreported exon, exon 1b, located between exons 1 and 2 of BST1. Inclusion of exon 1b in frame yields CD157-002, a novel proteoform of 333 aa: exclusion of exon 1b by alternative splicing generates canonical CD157, the dominant proteoform in neutrophils and other tissues analysed here. In comparative functional analyses, both proteoforms were indistinguishable in cell surface localization, specific mAb binding, and behaviour in cell adhesion and migration. However, NAD glycohydrolase activity was detected in canonical CD157 alone. Comparative phylogenetics indicate that exon 1b is a genomic innovation acquired during primate evolution, pointing to the importance of alternative splicing for CD157 function.