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Acknowledgments S.O. and A.C.S were recipient of a fellowship of Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina). V.B., I.E.P., E.M.V., F.C. and R.A. are members of Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina). This work was partially supported by Secretaría de Ciencia y Tecnología de la UNC (grant 05/C556), Consejo Nacional de Investigaciones Científicas y Técnicas (grant No. 11220110100775) and Agencia Nacional de Promoción Científica y Tecnológica (PICT redes 2007-01942) (Argentina). We thank Silvina Colla for linguistic revision of the manuscript.
Value of the data
Data In this data article, data are shared regarding protein stability and salt–polyethylene glycol (PEG) phase separation. The former is Rocilinostat spectra of Rp. viridis PRU [2,3] and RC, Rb. sphaeroides RC [4,5] and LH2, and Rb. capsulatus LH2 measured at different time points after addition of NaCl/PEG mixture. The latter is shown as minimum concentrations of salts and PEG that form immiscible aqueous phases [6] in the presence of 25mM Tris buffer and 8mg/mL N-octyl-β-d-glucoside.
Experimental design, materials and methods
Acknowledgements
Data Here we provide expression data for a focused set of lncRNAs during culture-induced differentiation of human CD34+ cells into erythroblasts (Table 1). We provide sequences for the cloned 5′ untranslated region (UTR) of Saf highlighting transcription factor binding sites including GATA-1, KLF1, and NF-κB, which were studied in detail in the research article (Fig. 1). We include relative transcript levels of GATA-1 and KLF1 in K562 human erythroleukemia cells and maturing human erythroblasts (Figs. 2 and 3). We share end point and quantitative RT-PCR analysis of cDNA prepared from total RNA isolated from human erythroblasts using random hexamers versus oligo(dT)18 (Fig. 4). Finally, we include flow cytometry histograms demonstrating Fas surface levels on maturing erythroblasts derived from human CD34+ cells transduced using mock conditions or Saf-encoding lentivirus particles (Fig. 5).
Experimental design, materials and methods
Acknowledgments We thank the flow cytometry laboratory of Melissa Roberts for expertize in flow cytometry. This work was supported by a Medical Innovators Grant from the Doris Duke Charitable Foundation (D.A.P. and A.W.). The Southern Illinois University School of Medicine flow cytometry equipment was supported by Award number S10RR025674 from the National Center for Research Resources. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Data The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository [2] with the dataset identifier PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD003105.
Experimental design, materials and methods The detailed method is described elsewhere [1].
Acknowledgments This work was supported in part by the Special Coordination Funds for Promoting Science and Technology, “Creation of Innovation Centers for Advanced Interdisciplinary Research Areas” in “Project for Developing Innovation Systems” Grant number 1800122 (to H.H.)., from the Ministry of Education, Culture, Sports, Science, and Technology, Japan. We thank Dr. Kentaro Yoshimatsu for his invaluable advice during this study.