individual protein band densitometry Search Results


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LI-COR odyssey infrared imaging systems software 2 1
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Bio-Rad quantity one software
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Fluorochem Ltd fluorochem hd2
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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NucleoTech Corporation gelexpert software
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Bio-Rad 620 scanning densitometer
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Bio-Rad individual protein bands
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Sangon Biotech peptide mass fingerprinting (pmf) analysis
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Proteome Factory AG identification of individual protein bands
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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TaKaRa recombinant egfp standard
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Bio-Rad imagelab
A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.
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Image Search Results


A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.

Journal: Bone

Article Title: Loss of Cbl-PI3K Interaction Modulates the Periosteal Response to Fracture by Enhancing Osteogenic Commitment and Differentiation

doi: 10.1016/j.bone.2016.11.020

Figure Lengend Snippet: A. Periosteal cell cultures were left untreated or were treated with 1 or 10 μm of LY294002 for 60 minutes. Total cell lysate (100 μg) was electrophoresed on 8 % SDS-PAGE. The blot was probed using anti-phospho AKT Thr 308 antibody (top), and then stripped and reprobed with anti-AKT (bottom) to verify equal loading of protein. The amounts of phosphorylated to total proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences), and the ratio of pAKT/AKT is indicated. A representative of two experiments is shown. B. Cells left untreated or treated with 40 μm of cycloheximide for 2, 4, 6 and 8 hours. Cell lysate (50 μg) were electrophoresed on 10 % SDS-PAGE. Blots were probed with anti-Osterix-antibodies (top) and anti-GAPDH antibodies (bottom) to verify equal protein loading. C. Bar graphs represent Osterix/GAPDH of three pooled experiments; * p<0.01 Vs. WT. D. Representative 20× fluorescent images of Osterix-expressing WT and YF periosteal cells counterstained with DAPI in the presence and absence of 10μm LY294002. White arrowheads point to cells in which Osterix is localized in the nucleus. E. Bar graphs represent the percent of periosteal cells with nuclear Osterix expression over total number of cells in the absence and presence of 1 and 10 μM LY294002. p* p<0.01 Vs. WT. A representative of 3 experiments is shown.

Article Snippet: The amounts of proteins in individual bands were quantified by using Odyssey Infrared Imaging Systems software 2.1 (LICOR Biosciences, Lincoln, NE) as previously reported [ 23 , 25 ].

Techniques: SDS Page, Imaging, Software, Expressing