c ebp α  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc c ebp α
    Western blotting was used to analyze the expression of adipogenic genes <t>C/EBP-α</t> in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
    C Ebp α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Epigallocatechin-3-gallate enhances the osteoblastogenic differentiation of human adipose-derived stem cells"

    Article Title: Epigallocatechin-3-gallate enhances the osteoblastogenic differentiation of human adipose-derived stem cells

    Journal: Drug Design, Development and Therapy

    doi: 10.2147/DDDT.S192683

    Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
    Figure Legend Snippet: Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.

    Techniques Used: Western Blot, Expressing, Cell Culture, Derivative Assay

    c ebp α  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc c ebp α
    Western blotting was used to analyze the expression of adipogenic genes <t>C/EBP-α</t> in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
    C Ebp α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Epigallocatechin-3-gallate enhances the osteoblastogenic differentiation of human adipose-derived stem cells"

    Article Title: Epigallocatechin-3-gallate enhances the osteoblastogenic differentiation of human adipose-derived stem cells

    Journal: Drug Design, Development and Therapy

    doi: 10.2147/DDDT.S192683

    Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
    Figure Legend Snippet: Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.

    Techniques Used: Western Blot, Expressing, Cell Culture, Derivative Assay

    anti c ebpα  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti c ebpα
    Anti C Ebpα, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti c ebp α  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti c ebp α
    DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the <t>C/EBP-</t> α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.
    Anti C Ebp α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Inhibition of Notch Signaling Promotes the Differentiation of Epicardial Progenitor Cells into Adipocytes"

    Article Title: Inhibition of Notch Signaling Promotes the Differentiation of Epicardial Progenitor Cells into Adipocytes

    Journal: Stem Cells International

    doi: 10.1155/2021/8859071

    DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the C/EBP- α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.
    Figure Legend Snippet: DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the C/EBP- α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.

    Techniques Used: Immunofluorescence, Staining, Cell Culture, Expressing, Reverse Transcription Polymerase Chain Reaction

    rabbit anti mouse c ebp α d56f10 monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti mouse c ebp α d56f10 monoclonal antibody
    Rabbit Anti Mouse C Ebp α D56f10 Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    c ebpα  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc c ebpα
    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, <t>C/EBPα</t> and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.
    C Ebpα, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Histone methyltransferase Smyd2 drives adipogenesis via regulating STAT3 phosphorylation"

    Article Title: Histone methyltransferase Smyd2 drives adipogenesis via regulating STAT3 phosphorylation

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-022-05321-7

    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: 3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Techniques Used: Transfection, Staining, Isolation, Expressing, Western Blot

    3T3-L1 preadipocytes or iWAT-SVF were treated with LLY-507 and meanwhile differentiated into mature adipocytes. A The Oil Red O staining of 3T3-L1 adipocytes. Magnification ×200. B The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) in 3T3-L1 adipocytes. C The protein expressions of adipogenesis markers (PPARγ, C/EBPα, and FABP4) in 3T3-L1 adipocytes treated with LLY-507 in a dose-dependent manner. D The Oil Red O staining of iWAT-SVF differentiated adipocytes. Magnification ×400. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα and Fabp4 ) in iWAT-SVF differentiated adipocytes. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) and the rate-limiting enzyme in adipogenesis (ACC and FASN) in iWAT-SVF differentiated adipocytes. Data are presented as mean ± SD. ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: 3T3-L1 preadipocytes or iWAT-SVF were treated with LLY-507 and meanwhile differentiated into mature adipocytes. A The Oil Red O staining of 3T3-L1 adipocytes. Magnification ×200. B The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) in 3T3-L1 adipocytes. C The protein expressions of adipogenesis markers (PPARγ, C/EBPα, and FABP4) in 3T3-L1 adipocytes treated with LLY-507 in a dose-dependent manner. D The Oil Red O staining of iWAT-SVF differentiated adipocytes. Magnification ×400. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα and Fabp4 ) in iWAT-SVF differentiated adipocytes. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) and the rate-limiting enzyme in adipogenesis (ACC and FASN) in iWAT-SVF differentiated adipocytes. Data are presented as mean ± SD. ** p < 0.01, *** p < 0.001.

    Techniques Used: Staining

    ccaat enhancer binding protein α c ebpα  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ccaat enhancer binding protein α c ebpα
    Ccaat Enhancer Binding Protein α C Ebpα, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti c ebp α  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti c ebp α
    a Mouse 3T3-L1 fibroblasts were treated with MDI induction medium (Diff.) or control vehicle. On Day 0, 3, 5, 7 after induction, cells were stained with Oil Red O and observed under microscopy. Bar = 60 µm. The amounts of lipid accumulation for individual culture plates were quantified by measuring absorbance at 490 nm (OD 490 ). Mean ± s.d. for six independent experiments. ** P < 0.01 and **** P < 0.0001 by two-way ANOVA analysis. b On the day after induction as indicated, Western blotting analyses revealed increased expressions of endogenous mouse stomatin (mSTOM), perilipin, PPAR γ and <t>C/EBP</t> α . c Subcellular distributions of stomatin and perilipin in Day 7 adipocyte-like cells were observed by differential interference contrast (DIC) and immunofluorescence (IF) microscopy using a confocal microscope. Cell nuclei (Nu) were revealed by Hoechst stain. Stomatin proteins were present on the plasma membranes (arrows) and surfaces of lipid droplet (LD) (inset i-iii). Bar = 10 µm. d STED microscopy showed that stomatin and perilipin were partially colocalized on the LD surfaces. Scale bar = 5 µm. e LDs were isolated and subjected to immunoblotting analyses. Stomatin and perilipin proteins, but not β-tubulin, were identified in the LD fractions (LD-1 & LD-2). Source data are provided as a Source data file. STED: stimulated emission depletion; T-1 & T-2: total cell lysates.
    Anti C Ebp α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth"

    Article Title: Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth

    Journal: Nature Communications

    doi: 10.1038/s41467-022-31825-z

    a Mouse 3T3-L1 fibroblasts were treated with MDI induction medium (Diff.) or control vehicle. On Day 0, 3, 5, 7 after induction, cells were stained with Oil Red O and observed under microscopy. Bar = 60 µm. The amounts of lipid accumulation for individual culture plates were quantified by measuring absorbance at 490 nm (OD 490 ). Mean ± s.d. for six independent experiments. ** P < 0.01 and **** P < 0.0001 by two-way ANOVA analysis. b On the day after induction as indicated, Western blotting analyses revealed increased expressions of endogenous mouse stomatin (mSTOM), perilipin, PPAR γ and C/EBP α . c Subcellular distributions of stomatin and perilipin in Day 7 adipocyte-like cells were observed by differential interference contrast (DIC) and immunofluorescence (IF) microscopy using a confocal microscope. Cell nuclei (Nu) were revealed by Hoechst stain. Stomatin proteins were present on the plasma membranes (arrows) and surfaces of lipid droplet (LD) (inset i-iii). Bar = 10 µm. d STED microscopy showed that stomatin and perilipin were partially colocalized on the LD surfaces. Scale bar = 5 µm. e LDs were isolated and subjected to immunoblotting analyses. Stomatin and perilipin proteins, but not β-tubulin, were identified in the LD fractions (LD-1 & LD-2). Source data are provided as a Source data file. STED: stimulated emission depletion; T-1 & T-2: total cell lysates.
    Figure Legend Snippet: a Mouse 3T3-L1 fibroblasts were treated with MDI induction medium (Diff.) or control vehicle. On Day 0, 3, 5, 7 after induction, cells were stained with Oil Red O and observed under microscopy. Bar = 60 µm. The amounts of lipid accumulation for individual culture plates were quantified by measuring absorbance at 490 nm (OD 490 ). Mean ± s.d. for six independent experiments. ** P < 0.01 and **** P < 0.0001 by two-way ANOVA analysis. b On the day after induction as indicated, Western blotting analyses revealed increased expressions of endogenous mouse stomatin (mSTOM), perilipin, PPAR γ and C/EBP α . c Subcellular distributions of stomatin and perilipin in Day 7 adipocyte-like cells were observed by differential interference contrast (DIC) and immunofluorescence (IF) microscopy using a confocal microscope. Cell nuclei (Nu) were revealed by Hoechst stain. Stomatin proteins were present on the plasma membranes (arrows) and surfaces of lipid droplet (LD) (inset i-iii). Bar = 10 µm. d STED microscopy showed that stomatin and perilipin were partially colocalized on the LD surfaces. Scale bar = 5 µm. e LDs were isolated and subjected to immunoblotting analyses. Stomatin and perilipin proteins, but not β-tubulin, were identified in the LD fractions (LD-1 & LD-2). Source data are provided as a Source data file. STED: stimulated emission depletion; T-1 & T-2: total cell lysates.

    Techniques Used: Staining, Microscopy, Western Blot, Immunofluorescence, Isolation

    a Mouse 3T3-L1 cells over-expressing human stomatin conjugated with RFP (hSTOM-RFP), or RFP as a control, were induced to differentiate. Lipid contents of the resulting adipocyte-like cells were stained and quantified. Mean ± s.d. for four experiments. Bar = 50 µm. b The protein of hSTOM, PPAR γ , C/EBP α , and perilipin were examined by Western blotting. c The numbers of LDs were counted and plotted as a function of LD sizes by the histogram. Large LDs (>80 µm 2 ) were more frequently found in hSTOM-RFP cells than control cells which contained mostly small (<40 µm 2 ) LDs. Mean ± s.e.m. for three experiments. * P < 0.05 by two-sided paired t -test. Bar = 100 µm. d The time-lapse recording of a representative LD-LD fusion event (black arrow) when a small LD (circled green) fused with a large LD (circled red). Image tiles in hr:min. Bar = 10 µm. e FRAP experiments were done on cells transfected with hSTOM-RFP or RFP. After pre-treating cells with Bodipy-FL-C 12 , fluorescence of a LD was photobleached (dashed box). Recovery of fluorescence, quantified as % of original intensity, was recorded at a 30-s interval. Mean ± s.e.m of LD. for three experiments. Bar = 10 µm. f In vitro assay for LD fusions. LDs isolated from adipocyte-like cells were pre-treated with either Bodipy-FL-C 16 or Bodipy-558/568-C 12 . Two LD suspension individually labeled red and green, were mixed in vitro in the presence of conditioned-medium (CM) prepared from 293 T cells over-expressing hSTOM-Flag (hSTOM), or empty control (Ctl). Excreted stomatin in CM was depleted by anti-hSTOM antibodies. g Most isolated LDs exhibited green- or red-fluorescence (arrowheads) alone; some LDs, however, contained both (arrows) as a result of LD fusions. Stomatin-containing CM increased LD fusion, while depletion of stomatin (hSTOM+Ab) inhibited fusion. Data represent six experiments. * P < 0.05 by two-sided paired student t-test. Source data are provided as a Source data file.
    Figure Legend Snippet: a Mouse 3T3-L1 cells over-expressing human stomatin conjugated with RFP (hSTOM-RFP), or RFP as a control, were induced to differentiate. Lipid contents of the resulting adipocyte-like cells were stained and quantified. Mean ± s.d. for four experiments. Bar = 50 µm. b The protein of hSTOM, PPAR γ , C/EBP α , and perilipin were examined by Western blotting. c The numbers of LDs were counted and plotted as a function of LD sizes by the histogram. Large LDs (>80 µm 2 ) were more frequently found in hSTOM-RFP cells than control cells which contained mostly small (<40 µm 2 ) LDs. Mean ± s.e.m. for three experiments. * P < 0.05 by two-sided paired t -test. Bar = 100 µm. d The time-lapse recording of a representative LD-LD fusion event (black arrow) when a small LD (circled green) fused with a large LD (circled red). Image tiles in hr:min. Bar = 10 µm. e FRAP experiments were done on cells transfected with hSTOM-RFP or RFP. After pre-treating cells with Bodipy-FL-C 12 , fluorescence of a LD was photobleached (dashed box). Recovery of fluorescence, quantified as % of original intensity, was recorded at a 30-s interval. Mean ± s.e.m of LD. for three experiments. Bar = 10 µm. f In vitro assay for LD fusions. LDs isolated from adipocyte-like cells were pre-treated with either Bodipy-FL-C 16 or Bodipy-558/568-C 12 . Two LD suspension individually labeled red and green, were mixed in vitro in the presence of conditioned-medium (CM) prepared from 293 T cells over-expressing hSTOM-Flag (hSTOM), or empty control (Ctl). Excreted stomatin in CM was depleted by anti-hSTOM antibodies. g Most isolated LDs exhibited green- or red-fluorescence (arrowheads) alone; some LDs, however, contained both (arrows) as a result of LD fusions. Stomatin-containing CM increased LD fusion, while depletion of stomatin (hSTOM+Ab) inhibited fusion. Data represent six experiments. * P < 0.05 by two-sided paired student t-test. Source data are provided as a Source data file.

    Techniques Used: Expressing, Staining, Western Blot, Transfection, Fluorescence, In Vitro, Isolation, Labeling

    a Stomatin knockdown was done by transduction of shRNA of Stomatin gene into 3T3-L1 cells generating shSTOM-1 cells or shSTOM-2 cells. After induction of adipogenic differentiation, shSTOM-1 and control cells were stained with Oil Red O. Cells after 7-day induction are shown using high-power microscopy. Bar = 20 µm. b On the day after induction as indicated, Western blotting analyses revealed decreased expression of mouse stomatin (mSTOM) by knockdown. Adipogenic proteins, including PPAR γ , and C/EBP α were also down-regulated. c On Day 7 of adipogenic differentiation, adipocyte-like shSTOM-1 cells were stained with Bodipy-FL and observed under differential interference contrast (DIC) and fluorescence (Flu) microscopy. The sizes of lipid droplets (LDs) were measured, and their numbers per 100 adipocytes were calculated. Histogram analyses showed more small LDs (<40 µm 2 ) and fewer large (>80 µm 2 ) LDs in shSTOM-1 cells than the control. Mean ± s.d. for three independent experiments. **** P < 0.0001 by two-way ANOVA. Bar = 20 μm. d Transcriptome analyses of adipocyte-like shSTOM-1 and control cells after induction for 7 days. From the data of microarray assays, scatter plots revealed enriched Wiki pathways in shSTOM-1 cells, compared to the control. For a given pathway, ratio of gene number being up- or down-regulated in that pathway were determined, and plotted as function of fold change. Each dot represents one gene. The color of the dots represents the range of P -values related to the indicated pathway are provided by the Transcriptome Analysis Console (TAC). e Heat map of adipogenesis gene obtained from the enrichment-based cluster analysis of the Wiki pathway. f Real-time qPCR analyses to validate the changed genes revealed by microarray assays. Data shown are fold changes relative to Nono mRNA level. Mean ± s.d. for three independent experiments. ** P < 0.01, *** P < 0.001, **** P < 0.0001 by multiple unpaired t -test. Source data are provided as a Source data file.
    Figure Legend Snippet: a Stomatin knockdown was done by transduction of shRNA of Stomatin gene into 3T3-L1 cells generating shSTOM-1 cells or shSTOM-2 cells. After induction of adipogenic differentiation, shSTOM-1 and control cells were stained with Oil Red O. Cells after 7-day induction are shown using high-power microscopy. Bar = 20 µm. b On the day after induction as indicated, Western blotting analyses revealed decreased expression of mouse stomatin (mSTOM) by knockdown. Adipogenic proteins, including PPAR γ , and C/EBP α were also down-regulated. c On Day 7 of adipogenic differentiation, adipocyte-like shSTOM-1 cells were stained with Bodipy-FL and observed under differential interference contrast (DIC) and fluorescence (Flu) microscopy. The sizes of lipid droplets (LDs) were measured, and their numbers per 100 adipocytes were calculated. Histogram analyses showed more small LDs (<40 µm 2 ) and fewer large (>80 µm 2 ) LDs in shSTOM-1 cells than the control. Mean ± s.d. for three independent experiments. **** P < 0.0001 by two-way ANOVA. Bar = 20 μm. d Transcriptome analyses of adipocyte-like shSTOM-1 and control cells after induction for 7 days. From the data of microarray assays, scatter plots revealed enriched Wiki pathways in shSTOM-1 cells, compared to the control. For a given pathway, ratio of gene number being up- or down-regulated in that pathway were determined, and plotted as function of fold change. Each dot represents one gene. The color of the dots represents the range of P -values related to the indicated pathway are provided by the Transcriptome Analysis Console (TAC). e Heat map of adipogenesis gene obtained from the enrichment-based cluster analysis of the Wiki pathway. f Real-time qPCR analyses to validate the changed genes revealed by microarray assays. Data shown are fold changes relative to Nono mRNA level. Mean ± s.d. for three independent experiments. ** P < 0.01, *** P < 0.001, **** P < 0.0001 by multiple unpaired t -test. Source data are provided as a Source data file.

    Techniques Used: Transduction, shRNA, Staining, Microscopy, Western Blot, Expressing, Fluorescence, Microarray

    a Dynamics expression patterns of stomatin, adipogenic genes C/EBP β , C/EBP δ , C/EBP α , and PPAR γ along the adipogenic differentiation process are depicted. Stomatin progressively increases during adipogenesis and may participate in modulation of other adipogenic gene. By inhibiting pERK, stomatin activates PPAR γ , as a prelude to adipogenesis. Stomatin may also directly activate PPAR γ pathway through currently unknown mechanisms. b Stomatin and calveolin-1 are known to associated with lipid raft (shadowed red). Stomatin proteins are present on the surfaces of LDs, together with perilipin. Stomatin can promote enlargement of LDs through facilitating LD-LD fusion (a → b → c). The presence of LCFAs outside the cell, through currently unknown mechanisms, relocates stomatin proteins from LDs to lipid rafts on the plasma membrane (1→2), where they interact with CD36 and possibly other FABPs, to promote uptake of LCFAs (3), resulting in increase of intracellular triglycerides, which are transported and stored in LDs (4).
    Figure Legend Snippet: a Dynamics expression patterns of stomatin, adipogenic genes C/EBP β , C/EBP δ , C/EBP α , and PPAR γ along the adipogenic differentiation process are depicted. Stomatin progressively increases during adipogenesis and may participate in modulation of other adipogenic gene. By inhibiting pERK, stomatin activates PPAR γ , as a prelude to adipogenesis. Stomatin may also directly activate PPAR γ pathway through currently unknown mechanisms. b Stomatin and calveolin-1 are known to associated with lipid raft (shadowed red). Stomatin proteins are present on the surfaces of LDs, together with perilipin. Stomatin can promote enlargement of LDs through facilitating LD-LD fusion (a → b → c). The presence of LCFAs outside the cell, through currently unknown mechanisms, relocates stomatin proteins from LDs to lipid rafts on the plasma membrane (1→2), where they interact with CD36 and possibly other FABPs, to promote uptake of LCFAs (3), resulting in increase of intracellular triglycerides, which are transported and stored in LDs (4).

    Techniques Used: Expressing

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    Cell Signaling Technology Inc c ebp α
    Western blotting was used to analyze the expression of adipogenic genes <t>C/EBP-α</t> in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
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    Western blotting was used to analyze the expression of adipogenic genes <t>C/EBP-α</t> in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.
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    DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the <t>C/EBP-</t> α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.
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    DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the <t>C/EBP-</t> α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.
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    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, <t>C/EBPα</t> and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.
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    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, <t>C/EBPα</t> and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.
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    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, <t>C/EBPα</t> and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.
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    Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.

    Journal: Drug Design, Development and Therapy

    Article Title: Epigallocatechin-3-gallate enhances the osteoblastogenic differentiation of human adipose-derived stem cells

    doi: 10.2147/DDDT.S192683

    Figure Lengend Snippet: Western blotting was used to analyze the expression of adipogenic genes C/EBP-α in hASCs cultured in various concentrations of EGCG for 14 days. Notes: ( A ) EGCG at all concentrations significantly suppressed the expression of C/EBP-α at day 14. The level of C/EBP-α expression was lowest in 10 μM EGCG. ( B ) C/EBP-α expression at day 14 of osteogenic induction. All data are presented as mean and SD. * p <0.05; ** p <0.01; and *** p <0.001 (N=3). Abbreviations: EGCG, epigallocatechin-3-gallate; hASCs, human adipose-derived stem cells.

    Article Snippet: Primary antibodies against osteocalcin (OCN; Sigma-Aldrich Co., catalog number: SAB1306277), bone sialoprotein (BSP, diluted 1:1,000; Cell Signaling Technology, Boston, MA, USA; catalog number 5468S), Runx2 (diluted 1:1,000; Cell Signaling Technology; catalog number 8486), STAT3 (diluted 1:1,000; Cell Signaling Technology; catalog number 9139), pSTAT3 (diluted 1:2,000; Cell Signaling Technology; catalog number 9145), PPAR-γ (diluted 1:1,000; Cell Signaling Technology; catalog number 2435), C/EBP-α (diluted 1:1,000; Cell Signaling Technology; catalog number 8178), and β-actin (diluted 1:1,000; Cell Signaling Technology; catalog number 4970) were incubated with the blots at 4°C overnight.

    Techniques: Western Blot, Expressing, Cell Culture, Derivative Assay

    DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the C/EBP- α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.

    Journal: Stem Cells International

    Article Title: Inhibition of Notch Signaling Promotes the Differentiation of Epicardial Progenitor Cells into Adipocytes

    doi: 10.1155/2021/8859071

    Figure Lengend Snippet: DAPT treatment upregulated the transcription factor PPAR- γ . (a, b) The crucial adipogenic transcription factors PPAR- γ and the C/EBP- α were determined by immunofluorescence staining after EPCs were cultured in adipogenic induction medium alone, with jagged-1 or with DAPT for 7 days. (c) The mRNA expression levels of PPAR- γ and C/EBP- α were determined by RT-PCR. (d, e) The adipocyte markers FABP-4 and perilipin-1 were determined by immunofluorescence. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (f) Lipid droplet accumulation was determined by Oil red O staining. EPCs were cultured in adipogenic induction medium with DAPT alone or combined with PPAR- γ antagonists. (g) The mRNA expression levels of adipocyte-related genes FABP4, perilipin-1, leptin, LPL, and adiponectin were determined by RT-PCR. The p values were calculated by t -test between 2 groups and by ANOVA among 3 groups. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 for pairwise comparison among the groups.

    Article Snippet: The cells were subsequently stained with the following antibodies: rabbit anti-Tbx18 (Abcam, Cat: ab115262), rabbit anti-Wt1 (Abcam, Cat: ab180840), rabbit anti-perilipin-1 (Abcam, Cat: ab3526), rabbit anti-FABP4 (fatty acid binding protein 4; Abcam, Cat: ab92501), rabbit anti-activated Notch-1 (Abcam, Cat: ab52301), mouse anti-Hes-1(Santa, Cat: sc-166410), rabbit anti-C/EBP- α (Cell signaling Technology, Cat: 8178T), rabbit anti-PPAR- γ (Cell signaling Technology, Cat: 2435T), rabbit anti- α -SMA (Abcam, Cat: ab124964), rabbit anti-Myh11 (Abcam, Cat: ab224804), and mouse anti-Periostin (Santa, Cat: sc-398631) at 4°C for at least 12 hours [ ].

    Techniques: Immunofluorescence, Staining, Cell Culture, Expressing, Reverse Transcription Polymerase Chain Reaction

    3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Journal: Cell Death & Disease

    Article Title: Histone methyltransferase Smyd2 drives adipogenesis via regulating STAT3 phosphorylation

    doi: 10.1038/s41419-022-05321-7

    Figure Lengend Snippet: 3T3-L1 preadipocytes or iWAT-SVF were transfected with Smyd2 siRNA or NC, followed by differentiation as described in the methods section. A The workflow for Smyd2 siRNA transfection and adipocyte differentiation. B The Oil Red O staining of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. Magnification × 200. C The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. D The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) of 3T3-L1 adipocytes with NC or Smyd2 siRNA transfection. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα, FABP4), the rate-limiting enzyme in adipogenesis (ACC and FASN) of iWAT-SVF adipocytes with NC or Smyd2 siRNA transfection. G The primary iWAT-SVF from WT and Smyd2 +/− mice were isolated and induced to undifferentiation or differentiation. Expression of Smyd2, adipogenesis markers (PPARγ, C/EBPα) and the rate-limiting enzymes in adipogenesis (ACC and FASN) were examined by western blot. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Article Snippet: Antibodies were obtained from the following commercial sources: Smyd2 (Proteintech, 21290-1-AP), p-JAK2 (Cell Signaling Technology, 3776S), p-STAT3 (Tyr705) (Cell Signaling Technology, 9134T), JAK2 (Cell Signaling Technology, 3230T), STAT3 (Cell Signaling Technology, 9139T), SOCS3 (Bioworld, BS60384), β-Tubulin (Proteintech, 66240-1-Ig), β-actin (Proteintech, 66009-1-Ig), Hsp90 (Proteintech, 13171-1-AP), C/EBPα (Cell Signaling Technology, 8178T), PPARγ (Cell Signaling Technology, 2435T), FABP4 (Cell Signaling Technology, 2120T), Fatty Acid Synthase (Cell Signaling Technology, 3180T), Acetyl-CoA Carboxylase (Cell Signaling Technology, 3676T).

    Techniques: Transfection, Staining, Isolation, Expressing, Western Blot

    3T3-L1 preadipocytes or iWAT-SVF were treated with LLY-507 and meanwhile differentiated into mature adipocytes. A The Oil Red O staining of 3T3-L1 adipocytes. Magnification ×200. B The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) in 3T3-L1 adipocytes. C The protein expressions of adipogenesis markers (PPARγ, C/EBPα, and FABP4) in 3T3-L1 adipocytes treated with LLY-507 in a dose-dependent manner. D The Oil Red O staining of iWAT-SVF differentiated adipocytes. Magnification ×400. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα and Fabp4 ) in iWAT-SVF differentiated adipocytes. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) and the rate-limiting enzyme in adipogenesis (ACC and FASN) in iWAT-SVF differentiated adipocytes. Data are presented as mean ± SD. ** p < 0.01, *** p < 0.001.

    Journal: Cell Death & Disease

    Article Title: Histone methyltransferase Smyd2 drives adipogenesis via regulating STAT3 phosphorylation

    doi: 10.1038/s41419-022-05321-7

    Figure Lengend Snippet: 3T3-L1 preadipocytes or iWAT-SVF were treated with LLY-507 and meanwhile differentiated into mature adipocytes. A The Oil Red O staining of 3T3-L1 adipocytes. Magnification ×200. B The mRNA levels of adipogenesis markers ( Pparγ , Cepbα , and Fabp4 ) in 3T3-L1 adipocytes. C The protein expressions of adipogenesis markers (PPARγ, C/EBPα, and FABP4) in 3T3-L1 adipocytes treated with LLY-507 in a dose-dependent manner. D The Oil Red O staining of iWAT-SVF differentiated adipocytes. Magnification ×400. E The mRNA levels of adipogenesis markers ( Pparγ , Cepbα and Fabp4 ) in iWAT-SVF differentiated adipocytes. F The protein expressions of adipogenesis markers (PPARγ, C/EBPα and FABP4) and the rate-limiting enzyme in adipogenesis (ACC and FASN) in iWAT-SVF differentiated adipocytes. Data are presented as mean ± SD. ** p < 0.01, *** p < 0.001.

    Article Snippet: Antibodies were obtained from the following commercial sources: Smyd2 (Proteintech, 21290-1-AP), p-JAK2 (Cell Signaling Technology, 3776S), p-STAT3 (Tyr705) (Cell Signaling Technology, 9134T), JAK2 (Cell Signaling Technology, 3230T), STAT3 (Cell Signaling Technology, 9139T), SOCS3 (Bioworld, BS60384), β-Tubulin (Proteintech, 66240-1-Ig), β-actin (Proteintech, 66009-1-Ig), Hsp90 (Proteintech, 13171-1-AP), C/EBPα (Cell Signaling Technology, 8178T), PPARγ (Cell Signaling Technology, 2435T), FABP4 (Cell Signaling Technology, 2120T), Fatty Acid Synthase (Cell Signaling Technology, 3180T), Acetyl-CoA Carboxylase (Cell Signaling Technology, 3676T).

    Techniques: Staining