Project description:3 samples of R1, R2 and R3 bone marrow monocytes were compared from 3 biological replicates in 3 separate experiments. R1, R2 and R3 were sorted from triplicate experiments from pools of mice
Project description:Samples ECL1_1260429_F1-F8 are TMT6plex samples fractionated into 8 fractions using the Pierce High pH Reversed-Phase Peptide Fractionation Kit. Samples are optic nerves protein lysates. Channels 126, 127, 128 are control samples (TFEBdPM-Halo) and channels 129, 130, 131 are mutant samples (Mog-Cre; TFEBdPM-Halo).
Samples 1251765_F1-F8 are TMT6plex samples fractionated into 8 fractions using the Pierce High pH Reversed-Phase Peptide Fractionation Kit. Samples are day 14 in vitro differentiated oligodendrocytes protein lysates. Channels 126, 127, 128 are control samples (TFEBdPM-Halo) and channels 129, 130, 131 are mutant samples (Mog-Cre; TFEBdPM-Halo).
Project description:Male and female collagen-enriched fraction of cartilage from bovine knees. Full thickness cartilage plugs without subchondral bone were digested with chondroitinase for 24 hours to remove proteoglycans. Cartilage was further decellularized with SDS.
LUM1_811145: channels 126, 127, 128 female, channels 129, 130, 131 male
LUM1_833734: channels 126, 127, 128 female, channels 129, 130, 131 male
Project description:Investigation of whole genome transcription expression level changes in Drosophila mojavensis wild-type populations (1 Punta Onah: PO, 2 Organ Pipe National Monument: OPNM, 3 Punta Prieta:PP, and 4 San Quintin: SQ). The experiment was designed to investigate functional genomic responses to temperature variation (15, 25, and 35 °C) in adult Drosophila mojavensis wild populations. For each treatment 1-5 replicates were used (R1, R2, R3, R4 & R5). SO and BC represents Sonora deserts and Baja California region respectively.
Project description:We reconstituted arrays of CTCF binding sites (L1, L2, L3, L4, R1, R2 and R3) and devised a synthetic topological insulator with tetO for chromatin-engineering (STITCH). By coupling STITCH with tetR linked to the KRAB domain to induce heterochromatin and disable the insulation, we developed a drug-inducible system to control gene activation by enhancers. We inserted STITCH into five different positions of the remaining allele of the locus: \\"STITCH+30kb\\", \\"STITCH+440kb\\", \\"STITCH+1760kb\\" and \\"STITCH+1790kb\\" have the STITCH insertions away from the MYC promoter for the indicated distances to the telomeric side of the p arm of the chromosome. \\"STITCH-30kb\\", at the 30-kb upstream from the MYC. We also made a deletion clone of the enhancer region, termed del(30-440). We made deletion of each CTCF array, L (delL) and R (delR), inversion of R (invR), deletion of the middle five binding sites from L2 to R2 (del(L2-R2)), and deletion of the six sites but for R3 (del(L1-R2)) in STITCH+30kb. We also obtained deletion and inversion of the whole of STITCH (del(L1-R3) and inv(L1-R3)). We integrated a transgene consisting of tetR-KRAB followed by DNA encoding the 2A peptide and the puromycin resistant gene with piggyBac transposition into the genome in the STITCH+30kb clone (STITCH/KRAB). We performed 4C-seq (Circular chromatin conformation capture assay followed by deep-sequencing) from the MYC promoter as a viewpoint to see how STITCH impacts on the chromatin conformation.
Project description:The mouse liver mitochondrial proteome was analysed in four different mouse groups (allocation of the samples to Exp1 and Exp2 in brackets): AL (ad libitum fed) C57Bl6 (Exp1 129, Exp1 130, Exp2 130), DR (dietary restriction) C57Bl6 (Exp1 126, Exp1 127, Exp1 128), AL ICRFa (Exp2 128, Exp2 129) and old ICRFa (Exp2 126, Exp2 127). To achieve quantitative standardisation between Exp1 and Exp2, all 10 samples were pooled and one portion of the pool was anlaysed in each Exp (Exp1 131 and Exp2 131). Following tryptic digest and TMT 6-plex labelling, samples were separated by OffGel electrophoresis and all fractions were subsequently analysed by LCMSMS on an Orbitrap LTQ XL. One survey scan (res. 30,000) was followed by a high energy HCD scan (res. 6000) and a low energy CID scan in the LTQ. HCD data were used for the quantitation and CID data for the identification of peptides. Data were searched using Mascot (v. 2.2) through the Proteome Discoverer interface. Peptide raw quantitations were extracted as text files and further processed using dpeaqms (http://r-forge.r-project.org/projects/dpeaqms/) to obtain probability values for the differences in protein amounts for specific proteins between the different animal groups.