Відмінності між версіями «The bar graph compares the densities of mRNA bands in each group expressed as a fold-change from levels in control mice which is represented by a line at 1-fold»
(Створена сторінка: The bar graph compares the [http://www.tradesparency.com/members/greek9puma/activity/98835/ Phosphorylated HSP-27 took longer to activate as its concentration s...) |
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| − | The bar graph compares the [http://www. | + | The bar graph compares the densities of mRNA bands in each team expressed as a fold-alter from stages in [http://www.sdlongzhou.net/comment/html/?120601.html The slides were mounted in Vectashield mounting medium containing DAPI (Vector Laboratories)] control mice which is represented by a line at 1-fold. We assayed phosphorylation of these two proteins in all groups of mice (Fig 6). The phosphorylation of Akt was increased 1.6-fold in control muscle and 2.0-fold in diabetic muscle by Acu-LFES treatment over those of diabetic mice that were not treated with Acu-LFES. The Thr32 phosphorylation of FoxO1 was increased 1.9-fold in Acu-LFES--treated non-diabetic mice and 1.8- fold in Acu-LFES--treated Fig 3. Acu-LFES counteracts diabetes-induced decrease of muscle regeneration proteins. Muscle proteins lysates were prepared from combined gastrocnemius and EDL muscles from control, Acu-LFES, diabetes or diabetes/Acu-LFES mice. Muscle regeneration related proteins (Pax7, myoD, myogenin, eMyHC) and GAPDH were measured by western blotting. The bar graph compares the protein band densities in each treatment group expressed as a fold-change from levels in control mice (represented by a line at 1-fold). All band densities were normalized to the density of GAPDH (Bars: mean s.e. n = 12/group = p |
Поточна версія на 06:32, 15 грудня 2016
The bar graph compares the densities of mRNA bands in each team expressed as a fold-alter from stages in The slides were mounted in Vectashield mounting medium containing DAPI (Vector Laboratories) control mice which is represented by a line at 1-fold. We assayed phosphorylation of these two proteins in all groups of mice (Fig 6). The phosphorylation of Akt was increased 1.6-fold in control muscle and 2.0-fold in diabetic muscle by Acu-LFES treatment over those of diabetic mice that were not treated with Acu-LFES. The Thr32 phosphorylation of FoxO1 was increased 1.9-fold in Acu-LFES--treated non-diabetic mice and 1.8- fold in Acu-LFES--treated Fig 3. Acu-LFES counteracts diabetes-induced decrease of muscle regeneration proteins. Muscle proteins lysates were prepared from combined gastrocnemius and EDL muscles from control, Acu-LFES, diabetes or diabetes/Acu-LFES mice. Muscle regeneration related proteins (Pax7, myoD, myogenin, eMyHC) and GAPDH were measured by western blotting. The bar graph compares the protein band densities in each treatment group expressed as a fold-change from levels in control mice (represented by a line at 1-fold). All band densities were normalized to the density of GAPDH (Bars: mean s.e. n = 12/group = p
