br Acknowledgments This work was supported by

Acknowledgments This work was supported by Grants from the Giovanni Armenise-Harvard Foundation Career Development Program, the Italian Association for Cancer Research (AIRC) (IG 11786), the Italian Ministry of Health (62/GR-2011-02347880) and the Epigen Flagship Project Grant (Conv. attuativa-Sottoprog. 6.7). The authors declare no conflict of interest.
Data, experimental design, materials and methods
Acknowledgment This study was supported by grants R01GM806171 and R01GM102538 from the National Institutes of Health to Yuan Chen, and included work performed in the Nuclear Magnetic Resonance and X-ray Crystallography Cores supported by the National Cancer Institute of the National Institutes of Health under award number P30CA33572. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
Data We compared the expression of 49 selected genes between human NSCs (hESC-derived hNSC H9 cells, Thermo Fisher) and normal human progenitor cells (nhNPCs, Lonza) following short-term culture under basal growth conditions. Q-PCR data was obtained for pluripotency genes, NSC, neuronal, astrocyte and oligodendrocyte lineage defining genes (n=21; Table 1.) (Fig. 1) with several of these markers also detected through immunofluorescence (IF) (Fig. 2) using specific liothyronine sodium cost (Table 3). In addition, Q-PCR data was obtained for 28 heparan and chondroitin sulphate proteoglycan biosynthesis enzymes and core protein genes (Table 2) ubiquitous to the neural niche [1–7] in hNSC H9 cells and nhNPCs (Figs. 3 and 4). The data presented provides information on self-renewal and multilineage potential as well as proteoglycan expression differences between the two neural stem/progenitor cell types.
Experimental design, materials and methods
Acknowledgements This work was supported through Queensland University of Technology postgraduate research awards (QUTPRA and IPRS) and the Estate of the late Clem Jones AO.
Specifications Table
Value of the data
Data Foodstuff, feed and agricultural samples were randomly collected from different sources, including local and imported materials from the Syrian local market to screen them for detecting the presence of GMOs using PCR, nested PCR- and multiplex PCR-based techniques using specific primers for the most commonly used foreign DNA commonly used in genetic transformation procedures, i.e., 35S promoter, T-nos, epsps, cryIA(b) gene and nptII gene [1–17].
Experimental design, materials and methods
Results
Acknowledgments
Data Data presented here describe the additional chemical analysis of poly(butylene adipate-co-butylene terephthalate [1–3] variants and oligomeric model substrates. 1H NMR spectra and 13C NMR spectra are provided showing the chemical structure and purity ob synthesized chemicals.
Experimental design, materials and methods
Acknowledgments This work has been supported by the Federal Ministry of Science, Research and Economy (BMWFW), the Federal Ministry of Traffic, Innovation and Technology (bmvit), the Styrian Business Promotion Agency SFG, the Standortagentur Tirol, the Government of Lower Austria and ZIT-Technology Agency of the City of Vienna through the COMET-Funding Program managed by the Austrian Research Promotion Agency FFG (Grant number 848951).
Specifications Table Value of the data Data Matrix metalloproteinases (MMPs) regulate the structural matrix environment and extracellular signaling by precise proteolytic cleavage. Unraveling complex in vivo proteolytic networks is challenging. Thus comprehensive specificity profiles of all proteases involved are needed to guide interpretation. The data in the ProteomeXchange archive (http://www.ebi.ac.uk/pride/archive/projects/PXD002265) and accompanying data of the present article provide a comprehensive resource for the individual assessment of the active site specificity of nine representative members of the human matrix metalloproteinase (MMP) family. The in-depth specificity comparison based on these proteomic data corroborated with kinetic analysis using a set of 6 quenched fluorescent peptides and in silico peptide docking was presented recently [1].