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  • 99
    Thermo Fisher anti glut 1 antibody
    Background subtracted OCT images of well plates containing <t>anti-Glut-1</t> tagged GNRs attached to Glut-1 protein suspended in PBS.
    Anti Glut 1 Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti glut 1 antibody/product/Thermo Fisher
    Average 99 stars, based on 30 article reviews
    Price from $9.99 to $1999.99
    anti glut 1 antibody - by Bioz Stars, 2020-08
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    98
    Millipore anti glut1
    <t>SLC2A1</t> <t>(GLUT1)</t> is a target of miR-150 in T cells
    Anti Glut1, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti glut1/product/Millipore
    Average 98 stars, based on 315 article reviews
    Price from $9.99 to $1999.99
    anti glut1 - by Bioz Stars, 2020-08
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    93
    Millipore glut1
    Levels of Glut 1 and Glut4, and glucose uptake in the skeletal muscle of RXRγ mice. ( A ) Gene expressions of RXRγ , <t>Glut1</t> , and 4 were examined by quantitative real-time PCR. The value for wild-type (littermates of line 4-3) mice was set at 100, and relative values are shown. ( B ) Protein levels of Glut1 and Glut4 were examined by Western blotting. Results of relative densitometric signal for Glut1 and 4 are shown. ( C ) Glucose uptake in the absence or presence of insulin and ( D ) glycogen content were increased in the skeletal muscle of RXRγ mice. Ratio of enhanced glucose uptake in the presence of insulin (insulin/basal) was similar in control and RXRγ mice. In A , B and D , the same samples were used. Mice were males of 12 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. These samples were also used in Table 1 . In C , mice were males of 24–27 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. * P
    Glut1, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 468 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glut1/product/Millipore
    Average 93 stars, based on 468 article reviews
    Price from $9.99 to $1999.99
    glut1 - by Bioz Stars, 2020-08
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    93
    Millipore glut1 antibody
    Akt activation is required for TRAF4-regulated glycolysis in human lung cancer. A and B, TRAF4 regulates glycolysis in A549 and H460 lung cancer cells. Western blotting was performed to detect <t>Glut1</t> and HK2 in sh-Mock and sh-TRAF4 cells (left). The levels
    Glut1 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glut1 antibody/product/Millipore
    Average 93 stars, based on 20 article reviews
    Price from $9.99 to $1999.99
    glut1 antibody - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

    93
    Millipore polyclonal glut1
    Akt activation is required for TRAF4-regulated glycolysis in human lung cancer. A and B, TRAF4 regulates glycolysis in A549 and H460 lung cancer cells. Western blotting was performed to detect <t>Glut1</t> and HK2 in sh-Mock and sh-TRAF4 cells (left). The levels
    Polyclonal Glut1, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal glut1/product/Millipore
    Average 93 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    polyclonal glut1 - by Bioz Stars, 2020-08
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    90
    R&D Systems human glut 1
    Roles of HSPGs, NRP-1, and <t>GLUT-1</t> in HTLV-3 Env-mediated entry. (A) CHO-K1 and CHO-K1-pgsA-745 cells were incubated overnight with MLV-based retroviral vectors pseudotyped with either HTLV-1 Env, HTLV-3 Env, or VSV-G and harvested 4 days later, and the
    Human Glut 1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human glut 1/product/R&D Systems
    Average 90 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    human glut 1 - by Bioz Stars, 2020-08
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    Image Search Results


    Background subtracted OCT images of well plates containing anti-Glut-1 tagged GNRs attached to Glut-1 protein suspended in PBS.

    Journal: Biosensors

    Article Title: Single Step Nanoplasmonic Immunoassay for the Measurement of Protein Biomarkers

    doi: 10.3390/bios3010077

    Figure Lengend Snippet: Background subtracted OCT images of well plates containing anti-Glut-1 tagged GNRs attached to Glut-1 protein suspended in PBS.

    Article Snippet: Optimization of Antibody Immobilization Protocol In order to determine the optimal procedure for anti-Glut-1 antibody and GNR conjugation, the supernatant solution generated during the centrifugal separation of Ab-GNR and unbound Glut-1 antibodies, was evaluated using NanoDrop optical spectrophotometer at 280 nm.

    Techniques:

    Calibration curve depicting averaged OCT signal intensity versus corresponding initial concentration of Glut-1 protein.

    Journal: Biosensors

    Article Title: Single Step Nanoplasmonic Immunoassay for the Measurement of Protein Biomarkers

    doi: 10.3390/bios3010077

    Figure Lengend Snippet: Calibration curve depicting averaged OCT signal intensity versus corresponding initial concentration of Glut-1 protein.

    Article Snippet: Optimization of Antibody Immobilization Protocol In order to determine the optimal procedure for anti-Glut-1 antibody and GNR conjugation, the supernatant solution generated during the centrifugal separation of Ab-GNR and unbound Glut-1 antibodies, was evaluated using NanoDrop optical spectrophotometer at 280 nm.

    Techniques: Concentration Assay

    Specificity study conducted using human vascular endothelial growth factor (VEGF) and BSA as competitive analytes for anti-Glut-1 tagged gold nanorods.

    Journal: Biosensors

    Article Title: Single Step Nanoplasmonic Immunoassay for the Measurement of Protein Biomarkers

    doi: 10.3390/bios3010077

    Figure Lengend Snippet: Specificity study conducted using human vascular endothelial growth factor (VEGF) and BSA as competitive analytes for anti-Glut-1 tagged gold nanorods.

    Article Snippet: Optimization of Antibody Immobilization Protocol In order to determine the optimal procedure for anti-Glut-1 antibody and GNR conjugation, the supernatant solution generated during the centrifugal separation of Ab-GNR and unbound Glut-1 antibodies, was evaluated using NanoDrop optical spectrophotometer at 280 nm.

    Techniques:

    SLC2A1 (GLUT1) is a target of miR-150 in T cells

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: CD46 activation regulates miR-150-mediated control of GLUT1 expression and cytokine secretion in human CD4+ T cells

    doi: 10.4049/jimmunol.1500516

    Figure Lengend Snippet: SLC2A1 (GLUT1) is a target of miR-150 in T cells

    Article Snippet: Anti-c-Myb (Millipore) and anti-β-actin (Abcam) were used in combination with goat anti-mouse-HRP secondary antibody (Dako), while anti-GLUT1 (Millipore) was used in combination with goat anti-rabbit-HRP (DAKO), and proteins visualised using ECL reagents (Santa Cruz) and a ChemiDoc CCD camera (BioRad).

    Techniques:

    Identification of the miR-150 seed site in SLC2A1

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: CD46 activation regulates miR-150-mediated control of GLUT1 expression and cytokine secretion in human CD4+ T cells

    doi: 10.4049/jimmunol.1500516

    Figure Lengend Snippet: Identification of the miR-150 seed site in SLC2A1

    Article Snippet: Anti-c-Myb (Millipore) and anti-β-actin (Abcam) were used in combination with goat anti-mouse-HRP secondary antibody (Dako), while anti-GLUT1 (Millipore) was used in combination with goat anti-rabbit-HRP (DAKO), and proteins visualised using ECL reagents (Santa Cruz) and a ChemiDoc CCD camera (BioRad).

    Techniques:

    Detection of glucose transporter 1 (GLUT1) in the aortic media. (A) GLUT1 expression (red) was assessed via immunofluorescence on aortic cross section of aneurysmal and non-aneurysmal specimens excised from patients with TAV (top row) or BAV (bottom row). The elastin autofluorescence appears in green and DAPI-stained nuclei are shown in blue. Scale bar = 50 μm. (B) Quantification of GLUT1 expression via western blot on aortic media lysates of non-aneurysmal (NA) and aneurysmal (TAA) specimens from TAV and BAV patients. The intensity of the band corresponding to GLUT1 (54 kDa) was normalized to that of β-actin. * indicates p

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Medial Hypoxia and Adventitial Vasa Vasorum Remodeling in Human Ascending Aortic Aneurysm

    doi: 10.3389/fcvm.2018.00124

    Figure Lengend Snippet: Detection of glucose transporter 1 (GLUT1) in the aortic media. (A) GLUT1 expression (red) was assessed via immunofluorescence on aortic cross section of aneurysmal and non-aneurysmal specimens excised from patients with TAV (top row) or BAV (bottom row). The elastin autofluorescence appears in green and DAPI-stained nuclei are shown in blue. Scale bar = 50 μm. (B) Quantification of GLUT1 expression via western blot on aortic media lysates of non-aneurysmal (NA) and aneurysmal (TAA) specimens from TAV and BAV patients. The intensity of the band corresponding to GLUT1 (54 kDa) was normalized to that of β-actin. * indicates p

    Article Snippet: After blocking for 1 h in blotting-grade blocker (BioRad), membranes were incubated overnight at 4°C with an anti-GLUT1 antibody (1:500, Millipore #07-1401), rinsed in PBS-Tween-20 0.1% and incubated for 2 h at room temperature with an anti-goat antibody coupled to horseradish peroxidase (Santa Cruz Biotechnology, #sc-2020).

    Techniques: Expressing, Immunofluorescence, Staining, Western Blot

    Knockdown of GLUT1 decreases de uptake and phototoxicity of PcGal 16 . Western blotting analysis and quantification of GLUT1 protein levels in HT-1376 and UM-UC-3 cells (panel A), in HT-1376 cells (panel E) or UM-UC-3 cells (panel F) after uptake with PcGal 16 in darkness and after PDT. β-actin was blotted as loading control. Quantitative analysis of GLUT1 (normalized to β-actin) expressed as a ratio of the levels found in HT-1376 cells (panel A). *(p

    Journal: PLoS ONE

    Article Title: Galactodendritic Phthalocyanine Targets Carbohydrate-Binding Proteins Enhancing Photodynamic Therapy

    doi: 10.1371/journal.pone.0095529

    Figure Lengend Snippet: Knockdown of GLUT1 decreases de uptake and phototoxicity of PcGal 16 . Western blotting analysis and quantification of GLUT1 protein levels in HT-1376 and UM-UC-3 cells (panel A), in HT-1376 cells (panel E) or UM-UC-3 cells (panel F) after uptake with PcGal 16 in darkness and after PDT. β-actin was blotted as loading control. Quantitative analysis of GLUT1 (normalized to β-actin) expressed as a ratio of the levels found in HT-1376 cells (panel A). *(p

    Article Snippet: Following electrophoresis and transfer to PVDF membranes (Bio-Rad, Hercules, CA, USA), the blots were incubated in 5% (m/v) nonfat milk in TBS-T (20 mM Tris, 150 mM NaCl, Tween 0.2%, pH 7.6) and probed with rabbit anti-galectin-1 1∶1,000 (Abcam, Cambridge, UK), rabbit anti-GLUT1 1∶1,000 (Chemicon, Boston, MA, USA) and mouse anti β-actin 1∶20,000 (Sigma) antibodies.

    Techniques: Western Blot

    Hypothetic illustration of phototoxicity of PcGal 16 in human bladder cancer cells. The uptake of PcGal 16 by bladder cancer cells is modulated by the presence of carbohydrate-binding proteins present at the cell surface ( i.e. GLUT1 and galectin-1). PcGal 16 is a nontoxic compound per se , and has high photocytotoxic efficiency against bladder cancer cell lines. Treatment with ROS quenchers demonstrated that cell death in bladder cancer cells is mediated by the production of ROS after PDT. Immediately after PDT with PcGal 16 there is an increase on the activity of antioxidant enzymes (SOD, CAT and GR antioxidant enzymes). The photoactivated PcGal 16 co-localizes with galectin-1 and GLUT1and reduces their levels.

    Journal: PLoS ONE

    Article Title: Galactodendritic Phthalocyanine Targets Carbohydrate-Binding Proteins Enhancing Photodynamic Therapy

    doi: 10.1371/journal.pone.0095529

    Figure Lengend Snippet: Hypothetic illustration of phototoxicity of PcGal 16 in human bladder cancer cells. The uptake of PcGal 16 by bladder cancer cells is modulated by the presence of carbohydrate-binding proteins present at the cell surface ( i.e. GLUT1 and galectin-1). PcGal 16 is a nontoxic compound per se , and has high photocytotoxic efficiency against bladder cancer cell lines. Treatment with ROS quenchers demonstrated that cell death in bladder cancer cells is mediated by the production of ROS after PDT. Immediately after PDT with PcGal 16 there is an increase on the activity of antioxidant enzymes (SOD, CAT and GR antioxidant enzymes). The photoactivated PcGal 16 co-localizes with galectin-1 and GLUT1and reduces their levels.

    Article Snippet: Following electrophoresis and transfer to PVDF membranes (Bio-Rad, Hercules, CA, USA), the blots were incubated in 5% (m/v) nonfat milk in TBS-T (20 mM Tris, 150 mM NaCl, Tween 0.2%, pH 7.6) and probed with rabbit anti-galectin-1 1∶1,000 (Abcam, Cambridge, UK), rabbit anti-GLUT1 1∶1,000 (Chemicon, Boston, MA, USA) and mouse anti β-actin 1∶20,000 (Sigma) antibodies.

    Techniques: Binding Assay, Activity Assay

    TAMs in human primary GBMs and xenografts are monocyte-derived macrophages from peripheral blood a, Immunofluorescent staining of CCR2 (the marker for monocyte-derived macrophages) and CX3CR1 (the microglia marker) in GBM xenograft and normal brain tissue. Frozen sections of GSC-derived tumor (T387) and the adjacent normal mouse brain were immunostained with antibodies against CCR2 (green) and CX3CR1 (red) and counterstained with DAPI (blue). CCR2 + cells were detected only in tumor tissue, while CX3CR1 + cells were detected only in normal brain. Scale bar, 40μm. b , Immunohistochemical staining of CCR2 and CX3CR1 in human primary GBMs and normal brain tissue. Two consecutive tissue microarray slides (US Biomax) containing GBMs and normal brain tissues were immunostained with antibody against CCR2 or CX3CR1 (brown) and counterstained with hematoxylin. GBM tumors showed abundant CCR2 + cells (the monocyte-derived TAMs) but not CX3CR1 + cells (microglia), while normal brain tissues contained CX3CR1 + cells but not CCR2 + cells. Scale bar, 40μm. c , Graphical analysis of ( b ) in tissue microarrays showed that CCR2 + cells (monocyte-derived TAMs) were detected in the majority (82.6%) of GBM cases (data from 23 tumors) and the minority (20%) of normal brains (data from 5 normal samples). In contrast, CX3CR1 + cells (microglia) were detected in all normal brains but only 4.3% of GBM tumor cases. d , Immunofluorescent staining of Iba1 and the CD31 in human primary GBMs. Frozen sections of a primary GBM (CW2445) were immunostained with antibodies against Iba1 to label TAMs (green) and CD31 to mark vessels (red) and counterstained with DAPI (blue). Abundant TAMs are enriched in perivascular niches. Scale bar, 80μm. e , Immunofluorescent staining of the TAM marker Iba1 and the endothelial marker Glut1 in GSC-derived xenografts. Frozen sections of GBM xenografts derived from GSCs (T387) were immunostained with antibodies against Iba1 (green) and Glut1 (red) and counterstained with DAPI (blue). TAMs (green) were localized near vessels but not in the area lacking blood vessel. Scale bar, 80μm.

    Journal: Nature cell biology

    Article Title: Periostin Secreted by Glioblastoma Stem Cells Recruits M2 Tumor-associated Macrophages and Promotes Malignant Growth

    doi: 10.1038/ncb3090

    Figure Lengend Snippet: TAMs in human primary GBMs and xenografts are monocyte-derived macrophages from peripheral blood a, Immunofluorescent staining of CCR2 (the marker for monocyte-derived macrophages) and CX3CR1 (the microglia marker) in GBM xenograft and normal brain tissue. Frozen sections of GSC-derived tumor (T387) and the adjacent normal mouse brain were immunostained with antibodies against CCR2 (green) and CX3CR1 (red) and counterstained with DAPI (blue). CCR2 + cells were detected only in tumor tissue, while CX3CR1 + cells were detected only in normal brain. Scale bar, 40μm. b , Immunohistochemical staining of CCR2 and CX3CR1 in human primary GBMs and normal brain tissue. Two consecutive tissue microarray slides (US Biomax) containing GBMs and normal brain tissues were immunostained with antibody against CCR2 or CX3CR1 (brown) and counterstained with hematoxylin. GBM tumors showed abundant CCR2 + cells (the monocyte-derived TAMs) but not CX3CR1 + cells (microglia), while normal brain tissues contained CX3CR1 + cells but not CCR2 + cells. Scale bar, 40μm. c , Graphical analysis of ( b ) in tissue microarrays showed that CCR2 + cells (monocyte-derived TAMs) were detected in the majority (82.6%) of GBM cases (data from 23 tumors) and the minority (20%) of normal brains (data from 5 normal samples). In contrast, CX3CR1 + cells (microglia) were detected in all normal brains but only 4.3% of GBM tumor cases. d , Immunofluorescent staining of Iba1 and the CD31 in human primary GBMs. Frozen sections of a primary GBM (CW2445) were immunostained with antibodies against Iba1 to label TAMs (green) and CD31 to mark vessels (red) and counterstained with DAPI (blue). Abundant TAMs are enriched in perivascular niches. Scale bar, 80μm. e , Immunofluorescent staining of the TAM marker Iba1 and the endothelial marker Glut1 in GSC-derived xenografts. Frozen sections of GBM xenografts derived from GSCs (T387) were immunostained with antibodies against Iba1 (green) and Glut1 (red) and counterstained with DAPI (blue). TAMs (green) were localized near vessels but not in the area lacking blood vessel. Scale bar, 80μm.

    Article Snippet: Specific antibodies against POSTN (Abcam, ab14041, 1: 400), GSC marker SOX2 (Millipore, AB5603, 1:200; Santa Cruz, sc-17320, 1:200) or OLIG2 (R & D systems, AF2418, 1:100), endothelial cell marker Glut1 (Millipore, 07-1401, 1:500) or CD31 (Dako, M082301, 1:100), and macrophage markers Iba1 (Abcam, ab5076, 1:200), CD11b (Abd serotec, MCA711GT, 1:100), Fizz1 (Abcam, ab39626, 1:100), CD163 (Santa Cruz, sc-33560, 1:100), F4/80 (Abd serotec, MCA497RT, 1:100), CX3CR1 (Abcam, ab8021, 1:100) or CCR2 (Abcam, ab32144, 1:100) were used for immunofluorescent staining on GBM tumor sections as indicated.

    Techniques: Derivative Assay, Staining, Marker, Immunohistochemistry, Microarray

    Tamoxifen decreases hypoxia and increases vascularization Immunofluorescence images of PDAC tissues from KPC mice treated with vehicle control of tamoxifen, scale bar 100 μm. (B, D) Quantification of GLUT1 (hypoxia marker) and CD31 (endothelial cell marker). Control ( n = 5), 2 mg ( n = 5), and 5 mg ( n = 4). In all cases, bars represent mean ± SEM. (C) Relative values of protein levels for Glut1 in PDAC tumors assessed by proteomic analysis (6 mice for control and 2 mg and 3 mice for 5 mg, and samples were analyzed in duplicates). Expression levels of DEGs relevant to response to hypoxia (left) and blood vessel morphogenesis (right). The values were normalized by tubulin family genes. Immunofluorescence images of PDAC tissues from KPC mice treated with vehicle control and 5 mg of tamoxifen, scale bar 100 μm. Quantification of HIF‐1A in PDAC tissues. Control ( n = 5) and 5 mg ( n = 4). In the box‐and‐whisker plot, the central box represents values from the lower to upper quartile. The middle line represents the mean. The vertical line extends from the minimum to the maximum value. qPCR levels of HIF‐1A in PSCs, normalized to RPLP0 and relative to control. Western blot bands for protein expression in PSCs (p‐Tmod is post‐translational modification). The plot shows the quantification of the sum of band intensities corresponding to isoform 1, isoform 2, isoform 3, and post‐transcriptionally modified HIF‐1A ( n = 8 control and n = 8 tam). Data information: All histogram bars represent mean ± SEM; * P

    Journal: EMBO Reports

    Article Title: Tamoxifen mechanically reprograms the tumor microenvironment via HIF‐1A and reduces cancer cell survival

    doi: 10.15252/embr.201846557

    Figure Lengend Snippet: Tamoxifen decreases hypoxia and increases vascularization Immunofluorescence images of PDAC tissues from KPC mice treated with vehicle control of tamoxifen, scale bar 100 μm. (B, D) Quantification of GLUT1 (hypoxia marker) and CD31 (endothelial cell marker). Control ( n = 5), 2 mg ( n = 5), and 5 mg ( n = 4). In all cases, bars represent mean ± SEM. (C) Relative values of protein levels for Glut1 in PDAC tumors assessed by proteomic analysis (6 mice for control and 2 mg and 3 mice for 5 mg, and samples were analyzed in duplicates). Expression levels of DEGs relevant to response to hypoxia (left) and blood vessel morphogenesis (right). The values were normalized by tubulin family genes. Immunofluorescence images of PDAC tissues from KPC mice treated with vehicle control and 5 mg of tamoxifen, scale bar 100 μm. Quantification of HIF‐1A in PDAC tissues. Control ( n = 5) and 5 mg ( n = 4). In the box‐and‐whisker plot, the central box represents values from the lower to upper quartile. The middle line represents the mean. The vertical line extends from the minimum to the maximum value. qPCR levels of HIF‐1A in PSCs, normalized to RPLP0 and relative to control. Western blot bands for protein expression in PSCs (p‐Tmod is post‐translational modification). The plot shows the quantification of the sum of band intensities corresponding to isoform 1, isoform 2, isoform 3, and post‐transcriptionally modified HIF‐1A ( n = 8 control and n = 8 tam). Data information: All histogram bars represent mean ± SEM; * P

    Article Snippet: Sections were incubated with primary antibodies against GLUT1 (Merk Millipore, UK; 07‐1401 1/500) and CD31 (Abcam, Cambridge, UK; ab56299 1/200) in 1% BSA and 0.3% Triton X‐100 (both from Sigma‐Aldrich, St. Louis, MO) overnight at 4°C.

    Techniques: Immunofluorescence, Mouse Assay, Marker, Expressing, Whisker Assay, Real-time Polymerase Chain Reaction, Western Blot, Modification

    SFN modulate the redox-metabolic interplay of the brain vascular endothelium to promote ATP production. SFN promotes upregulation of Glut1 expression ( A ) and transport activity ( B ) as determined by 2-NBDG uptake normalized to total protein. ( C ) Key genes involved in the regulation of glycolysis were also upregulated including hexokinase 1 ( Ht1 ) and pyruvate kinase 2 ( Pkm2 ) as analyzed by MitoChip array ( C1 ) and confirmed by RT-PCR ( C2 ). The overall cellular effect was a substantial increase in ATP production ( D ). N = 3 independent biological samples per condition assayed in triplicates. “ * ”p

    Journal: Scientific Reports

    Article Title: In Vitro Modulation of Redox and Metabolism Interplay at the Brain Vascular Endothelium: Genomic and Proteomic Profiles of Sulforaphane Activity

    doi: 10.1038/s41598-018-31137-7

    Figure Lengend Snippet: SFN modulate the redox-metabolic interplay of the brain vascular endothelium to promote ATP production. SFN promotes upregulation of Glut1 expression ( A ) and transport activity ( B ) as determined by 2-NBDG uptake normalized to total protein. ( C ) Key genes involved in the regulation of glycolysis were also upregulated including hexokinase 1 ( Ht1 ) and pyruvate kinase 2 ( Pkm2 ) as analyzed by MitoChip array ( C1 ) and confirmed by RT-PCR ( C2 ). The overall cellular effect was a substantial increase in ATP production ( D ). N = 3 independent biological samples per condition assayed in triplicates. “ * ”p

    Article Snippet: Mouse anti-Glut1 (clone 5B12.3) from EMD Millipore (Billerica, MA); Mini-Protean® TGXTM gels for western blotting were purchased from Bio-rad (Hercules, CA, USA).

    Techniques: Expressing, Activity Assay, Reverse Transcription Polymerase Chain Reaction

    A) Representative western blots and B) quantification of glucose transporters Glut4 and Glut1 in controls (Ctr), SHR-lean and SHR-ob (n = 6 each). GAPDH was used as a loading control. Data are presented in means ± SEM.

    Journal: Journal of Translational Medicine

    Article Title: Cardiac remodeling and myocardial dysfunction in obese spontaneously hypertensive rats

    doi: 10.1186/1479-5876-10-187

    Figure Lengend Snippet: A) Representative western blots and B) quantification of glucose transporters Glut4 and Glut1 in controls (Ctr), SHR-lean and SHR-ob (n = 6 each). GAPDH was used as a loading control. Data are presented in means ± SEM.

    Article Snippet: Membranes were blocked in Tris-buffered saline (TBS) containing 5% nonfat dry milk for 120 min at room temperature and exposed to rabbit polyclonal anti-phospho-phospholamban Thr17 (sc-17024-R, Santa Cruz Biotechnology, CA, USA; dilution: 1:400), rabbit polyclonal anti-phospho-phospholamban Ser16 (#07-052, Upstate, Millipore: dilution: 1:400), mouse monoclonal anti-Phospholamban (#05-205, Millipore: dilution: 1:500), anti-goat polyclonal Serca2 (N-19, sc-8095, Santa Cruz, 1:1000), anti-mouse Glut4 (Cell Signaling; #2213S, 1:1000), anti-rabbit Glut1 (Millipore; #07-1401, 1:1000) and mouse monoclonal IgG GAPDH (6C5: sc-32233, Santa Cruz Biotechnology, 1:5000).

    Techniques: Western Blot

    Immunodetection of GLUT1 in the mouse cerebellar cortex on postnatal day (P)7 (A), P15 (B), P21 (C) and in adults (D). EGL, external granule cell layer; IGL, internal granule cell layer; ML, molecular layer; PL, Purkinje cell layer. GLUT1 immunoreactivity

    Journal: Journal of Anatomy

    Article Title: Developmental regulation of glucose transporters GLUT3, GLUT4 and GLUT8 in the mouse cerebellar cortex

    doi: 10.1111/j.1469-7580.2010.01291.x

    Figure Lengend Snippet: Immunodetection of GLUT1 in the mouse cerebellar cortex on postnatal day (P)7 (A), P15 (B), P21 (C) and in adults (D). EGL, external granule cell layer; IGL, internal granule cell layer; ML, molecular layer; PL, Purkinje cell layer. GLUT1 immunoreactivity

    Article Snippet: Rabbit anti-GLUT4 and rabbit anti-GLUT1 antibodies were obtained from Calbiochem.

    Techniques: Immunodetection

    Levels of Glut 1 and Glut4, and glucose uptake in the skeletal muscle of RXRγ mice. ( A ) Gene expressions of RXRγ , Glut1 , and 4 were examined by quantitative real-time PCR. The value for wild-type (littermates of line 4-3) mice was set at 100, and relative values are shown. ( B ) Protein levels of Glut1 and Glut4 were examined by Western blotting. Results of relative densitometric signal for Glut1 and 4 are shown. ( C ) Glucose uptake in the absence or presence of insulin and ( D ) glycogen content were increased in the skeletal muscle of RXRγ mice. Ratio of enhanced glucose uptake in the presence of insulin (insulin/basal) was similar in control and RXRγ mice. In A , B and D , the same samples were used. Mice were males of 12 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. These samples were also used in Table 1 . In C , mice were males of 24–27 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. * P

    Journal: PLoS ONE

    Article Title: Increased Systemic Glucose Tolerance with Increased Muscle Glucose Uptake in Transgenic Mice Overexpressing RXR? in Skeletal Muscle

    doi: 10.1371/journal.pone.0020467

    Figure Lengend Snippet: Levels of Glut 1 and Glut4, and glucose uptake in the skeletal muscle of RXRγ mice. ( A ) Gene expressions of RXRγ , Glut1 , and 4 were examined by quantitative real-time PCR. The value for wild-type (littermates of line 4-3) mice was set at 100, and relative values are shown. ( B ) Protein levels of Glut1 and Glut4 were examined by Western blotting. Results of relative densitometric signal for Glut1 and 4 are shown. ( C ) Glucose uptake in the absence or presence of insulin and ( D ) glycogen content were increased in the skeletal muscle of RXRγ mice. Ratio of enhanced glucose uptake in the presence of insulin (insulin/basal) was similar in control and RXRγ mice. In A , B and D , the same samples were used. Mice were males of 12 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. These samples were also used in Table 1 . In C , mice were males of 24–27 weeks of age. The number of animals was 6 for both control (open bars) and RXRγ (filled bars) mice. * P

    Article Snippet: We also observed that Glut1 is significantly increased in RXRγ mice at the protein level (P < 0.05), with no significant difference in Glut4 between genotypes ( ).

    Techniques: Mouse Assay, Real-time Polymerase Chain Reaction, Western Blot

    Transient transfection-reporter assay of the effect of RXRγ on Glut1 promoter. ( A ) Glut1 -Luc plasmid, with or without RXRγ and/or PPARδ expression vectors, was transfected into the quadriceps muscle of C57BL6 mice. Activation of the luciferase reporter gene was measured in relative light units and normalized to dual luciferase activity. Mean values from experiments (n = 5) are shown as fold induction, where the activity in the absence of RXRγ is the reference value (set at 100). ( B ) Schematic representations of serial deletion of Glut1 promoter constructs are shown in the figure. Squares denote the putative PPAR/RXR binding sites. Open bars; Glut1 -Luc without RXRγ and PPARδ expression vectors, and filled bars; Glut1 -Luc with RXRγ and PPARδ expression vectors. The activity in the absence of RXRγ and PPARδ in each experiment for different Glut1 -Luc construct in the reference value (set at 100). ** P

    Journal: PLoS ONE

    Article Title: Increased Systemic Glucose Tolerance with Increased Muscle Glucose Uptake in Transgenic Mice Overexpressing RXR? in Skeletal Muscle

    doi: 10.1371/journal.pone.0020467

    Figure Lengend Snippet: Transient transfection-reporter assay of the effect of RXRγ on Glut1 promoter. ( A ) Glut1 -Luc plasmid, with or without RXRγ and/or PPARδ expression vectors, was transfected into the quadriceps muscle of C57BL6 mice. Activation of the luciferase reporter gene was measured in relative light units and normalized to dual luciferase activity. Mean values from experiments (n = 5) are shown as fold induction, where the activity in the absence of RXRγ is the reference value (set at 100). ( B ) Schematic representations of serial deletion of Glut1 promoter constructs are shown in the figure. Squares denote the putative PPAR/RXR binding sites. Open bars; Glut1 -Luc without RXRγ and PPARδ expression vectors, and filled bars; Glut1 -Luc with RXRγ and PPARδ expression vectors. The activity in the absence of RXRγ and PPARδ in each experiment for different Glut1 -Luc construct in the reference value (set at 100). ** P

    Article Snippet: We also observed that Glut1 is significantly increased in RXRγ mice at the protein level (P < 0.05), with no significant difference in Glut4 between genotypes ( ).

    Techniques: Transfection, Reporter Assay, Plasmid Preparation, Expressing, Mouse Assay, Activation Assay, Luciferase, Activity Assay, Construct, Binding Assay

    Akt activation is required for TRAF4-regulated glycolysis in human lung cancer. A and B, TRAF4 regulates glycolysis in A549 and H460 lung cancer cells. Western blotting was performed to detect Glut1 and HK2 in sh-Mock and sh-TRAF4 cells (left). The levels

    Journal: Cancer research

    Article Title: TRAF4 is a critical molecule for Akt activation in lung cancer

    doi: 10.1158/0008-5472.CAN-13-0913

    Figure Lengend Snippet: Akt activation is required for TRAF4-regulated glycolysis in human lung cancer. A and B, TRAF4 regulates glycolysis in A549 and H460 lung cancer cells. Western blotting was performed to detect Glut1 and HK2 in sh-Mock and sh-TRAF4 cells (left). The levels

    Article Snippet: The Glut1 antibody was obtained from Millipore (Billerica, MA) and anti-E-cadherin was from BD Biosciences (San Jose, CA).

    Techniques: Activation Assay, Western Blot

    Roles of HSPGs, NRP-1, and GLUT-1 in HTLV-3 Env-mediated entry. (A) CHO-K1 and CHO-K1-pgsA-745 cells were incubated overnight with MLV-based retroviral vectors pseudotyped with either HTLV-1 Env, HTLV-3 Env, or VSV-G and harvested 4 days later, and the

    Journal:

    Article Title: The Receptor Complex Associated with Human T-Cell Lymphotropic Virus Type 3 (HTLV-3) Env-Mediated Binding and Entry Is Distinct from, but Overlaps with, the Receptor Complexes of HTLV-1 and HTLV-2 ▿

    doi: 10.1128/JVI.02285-08

    Figure Lengend Snippet: Roles of HSPGs, NRP-1, and GLUT-1 in HTLV-3 Env-mediated entry. (A) CHO-K1 and CHO-K1-pgsA-745 cells were incubated overnight with MLV-based retroviral vectors pseudotyped with either HTLV-1 Env, HTLV-3 Env, or VSV-G and harvested 4 days later, and the

    Article Snippet: The level of GLUT-1 expression was determined using two antibodies which recognize extracellular domains of human GLUT-1: a mouse anti-human monoclonal antibody from R & D Systems (MAB1418) and a rabbit anti-human polyclonal from Alpha Diagnostics (GT14-A), as previously described ( ).

    Techniques: Incubation

    Contribution of GLUT-1 to HTLV-3 SU binding. (A) The cell surface levels of HSPG, NRP-1, and GLUT-1 on U87 clones C5 (GLUT-1 + ) and C8 (GLUT-1 Low ) were determined by flow cytometry, as in Fig. . Black line, specific antibodies;

    Journal:

    Article Title: The Receptor Complex Associated with Human T-Cell Lymphotropic Virus Type 3 (HTLV-3) Env-Mediated Binding and Entry Is Distinct from, but Overlaps with, the Receptor Complexes of HTLV-1 and HTLV-2 ▿

    doi: 10.1128/JVI.02285-08

    Figure Lengend Snippet: Contribution of GLUT-1 to HTLV-3 SU binding. (A) The cell surface levels of HSPG, NRP-1, and GLUT-1 on U87 clones C5 (GLUT-1 + ) and C8 (GLUT-1 Low ) were determined by flow cytometry, as in Fig. . Black line, specific antibodies;

    Article Snippet: The level of GLUT-1 expression was determined using two antibodies which recognize extracellular domains of human GLUT-1: a mouse anti-human monoclonal antibody from R & D Systems (MAB1418) and a rabbit anti-human polyclonal from Alpha Diagnostics (GT14-A), as previously described ( ).

    Techniques: Binding Assay, Clone Assay, Flow Cytometry, Cytometry