Composition and nutrient level of diets (as fed basis).

a<p>Providing the following per mg/kg diet: retinyl acetate, 3.44; cholecalciferol, 0.075; all-rac-α-tocopherol acetate, 30; menadione, 1.3; thiamin, 2.2; riboflavin, 8; nicotinamide, 40; choline chloride, 600; calcium pantothenate, 10; pyridoxine·HCl, 4; biotin, 0.04; folic acid, 1; cobalamin, 0.013; Fe (as FeSO₄.H₂O), 80; Cu (as CuSO₄.5H₂O), 8; Mn (as MnSO₄.H₂O), 110; Zn (as ZnO), 65; I (as KIO₃), 1.1; Se (as Na₂SeO₃), 0.3.</p><p>Composition and nutrient level of diets (as fed basis).</p

Myostatin (MSTN) mRNA level and DNA methylation of gene exon 1 region.

<p>Heavy −48.3±0.1 g; Light −41.7±0.1 g; CM – control methionine levels (0.50% and 0.43% methionine during 1–21 d and 22–42 d, respectively); HM - high methionine levels (0.60% and 0.53% methionine during 1–21 d and 22–42 d, respectively); HW - hatching weight.</p><p>SEM - standard error of the mean.</p><p>Within the same row, different superscripts indicate significant differences (<i>P</i><0.05).</p><p>Myostatin (MSTN) mRNA level and DNA methylation of gene exon 1 region.</p

Phosphorylation of ERK1/2, mTOR and FoxO4.

<p>Western blot analysis (up) and quantification of the results (down) are shown. H - heavy (48.3±0.1 g); L - light (41.7±0.1 g); CM – control methionine levels (0.50% and 0.43% methionine during 1–21 d and 22–42 d, respectively); HM - high methionine levels (0.60% and 0.53% methionine during 1–21 d and 22–42 d, respectively). Different superscripts indicate significant differences (<i>P</i><0.05).</p

Foi et vie : revue de quinzaine, religieuse, morale, littéraire, sociale

01 février 19071907/02/01 (A10,N3)-1907/02/01

Additional file 1: of Effects of dietary Bacillus amyloliquefaciens supplementation on growth performance, intestinal morphology, inflammatory response, and microbiota of intra-uterine growth retarded weanling piglets

Availability of data and materials. (XLSX 32 kb

Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs.

<p>WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0090615#s2" target="_blank">Methods</a>). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the BioLegend Rb pAb.</p

rNanogP8 protein ID using IP and mass spectrometry.

<p>(<b>A</b>) IP in rNanogP8 proteins using the SC pAb H-155 followed by WB using the R& D goat pAb. RbIgG was used as the control Ab. Red arrowhead, the 42 kD band; green arrowhead, the faster migrating major band in MCF7 rNanogP8; IgH, IgG heavy chain. (<b>B</b>) IP using the R&D goat pAb followed by WB using the eBioscience mAb. Goat IgG was used as the control Ab. Red arrowhead, the 42 kD band; green arrowheads, the two lower bands; IgH, IgG heavy chain. In this experiment, NTERA-2 NE and cytosol and HPCa rNanogP8 were also loaded in WB analysis. (<b>C–D</b>) Mass spectrometry ID of rNanogP8 proteins. The HPCa5 rNanogP8 protein made in pET-28b was used in IP with either H-155 or Kamiya Rb pAb (RbIgG as the Ab control). The immunoprecipitates were subjected to SDS-PAGE, stained with SYPRO Ruby, and 9 bands (rN1 - rN9) cut out for protein ID (C). M, protein marker. The identified peptides were presented in D. (<b>E–F</b>) Mass spectrometry ID of rNanogP8 proteins in a separate experiment using conditions as above. Four bands (RH1–RH4) were cut out for protein ID (E) and identified peptides presented in F.</p

Examples of Nanog antibodies and their recognized protein bands.

<p>*This table lists the information for the 8 antibodies used in our current study, together with several others commercial and home-made antibodies. Shown in parenthesis are catalog numbers.</p><p><b>Abbreviations</b>: EC, embryonal carcinoma; EG, embryonic germ cells; hESCs, human embryonic stem cells; hNanog,</p><p>human Nanog; mESCs, mouse embryonic stem cells; mAb, monoclonal antibody; mNanog, mouse Nanog protein;</p><p>pAb, polyclonal antibody; Rb, rabbit; rhNanog, recombinant human Nanog protein; SC, Santa Cruz.</p

WB analysis of endogenous Nanog1 protein species in NTERA-2 cells.

<p>(<b>A</b>) Schematic of the human Nanog protein and 8 anti-Nanog Abs used in this study. Shown in parentheses are epitopes of individual Abs. ND, N-terminus domain; HD, homeodomain; CD1 and CD2, C-terminus domain 1 and 2; WR, tryptophan-rich domain. The asterisk in ND indicates the Leu61 residue recognized by the eBioscience mAb (arrow) mapped from our present studies. (B–H) WB analysis in NTERA-2 NE (N, two different batches) or cytosol (C) using 8 anti-Nanog Abs. Individual Ab is indicated at the bottom and M.W on the left. Black arrowhead, the predicted 35 kD Nanog protein; red arrowhead, the main 42 kD band; green arrows, additional bands (especially after longer exposures).</p

Nanog proteins in NTERA-2 human EC cells.^*

<p>*Presented are the results of various experiments using the 8 anti-Nanog Abs. The Biolegend Ab is the only Ab that does not recognize the 42 kD band as the major protein band and does not recognize the 35 kD band. Presented molecular masses are all estimated based on their migrations on SDS-PAGE.</p