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glut-4 protein  (Merck KGaA)

 
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    Structured Review

    Merck KGaA glut-4 protein
    Glut 4 Protein, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/glut-4+protein/antibodies+against+glut4/pmc08100388-59-28-32
    Average 90 stars, based on 1 article reviews
    glut-4 protein - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Clinical Proteomics:

    Article Title: Decreased muscle‐derived musclin by chronic resistance exercise is associated with improved insulin resistance in rats with type 2 diabetes
    Article Snippet: Before being used as the plasma membrane fraction, the homogenate was centrifuged briefly, and the supernatant was centrifuged for 1 h at 215,000 g . The levels of GLUT‐4 protein (# 07–1404; Merck Millipore) were measured in both the cytosol and membrane proteins via western blotting analysis.

    Membrane:

    Article Title: Decreased muscle‐derived musclin by chronic resistance exercise is associated with improved insulin resistance in rats with type 2 diabetes
    Article Snippet: Before being used as the plasma membrane fraction, the homogenate was centrifuged briefly, and the supernatant was centrifuged for 1 h at 215,000 g . The levels of GLUT‐4 protein (# 07–1404; Merck Millipore) were measured in both the cytosol and membrane proteins via western blotting analysis.

    Western Blot:

    Article Title: Decreased muscle‐derived musclin by chronic resistance exercise is associated with improved insulin resistance in rats with type 2 diabetes
    Article Snippet: Before being used as the plasma membrane fraction, the homogenate was centrifuged briefly, and the supernatant was centrifuged for 1 h at 215,000 g . The levels of GLUT‐4 protein (# 07–1404; Merck Millipore) were measured in both the cytosol and membrane proteins via western blotting analysis.



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    Image Search Results


    A–D, quantitative real-time RT-PCR analyses of adiponectin mRNA (A) and its receptors 1 (AdipoR1) and 2 (AdipoR2) mRNAs (B) in EP fat; Western blot analyses of phosphorylation of AMPK, phosphorylation of ACC, IRS-1 and PPARα protein levels using β-actin as a loading control (C); quantitative real-time RT-PCR analysis of Glut-4 mRNA in EP fat (D). All values are presented as means ± SEM, n = 4–6 mice per group. * P <0.05, ** P <0.01 vs. control mice treated with DMSO. E–F, both basal and insulin-stimulated Glut-4 membrane translocations detected by Western blotting using β-actin as a loading control (E); and immunofluorescence detection of membrane Glut-4 (F, ×1000 magnification). Values are presented as means ± SEM, n = 4 mice per group injected i.p. with insulin or saline, * P <0.05 as indicated.

    Journal: PLoS ONE

    Article Title: Regulation of Insulin Resistance and Adiponectin Signaling in Adipose Tissue by Liver X Receptor Activation Highlights a Cross-Talk with PPARγ

    doi: 10.1371/journal.pone.0101269

    Figure Lengend Snippet: A–D, quantitative real-time RT-PCR analyses of adiponectin mRNA (A) and its receptors 1 (AdipoR1) and 2 (AdipoR2) mRNAs (B) in EP fat; Western blot analyses of phosphorylation of AMPK, phosphorylation of ACC, IRS-1 and PPARα protein levels using β-actin as a loading control (C); quantitative real-time RT-PCR analysis of Glut-4 mRNA in EP fat (D). All values are presented as means ± SEM, n = 4–6 mice per group. * P <0.05, ** P <0.01 vs. control mice treated with DMSO. E–F, both basal and insulin-stimulated Glut-4 membrane translocations detected by Western blotting using β-actin as a loading control (E); and immunofluorescence detection of membrane Glut-4 (F, ×1000 magnification). Values are presented as means ± SEM, n = 4 mice per group injected i.p. with insulin or saline, * P <0.05 as indicated.

    Article Snippet: Membranes were then incubated with primary antibodies (diluted 1∶1,000) including anti-rabbit p-AMPK, AMPK, p-ACC, ACC, PPARα, IRS-1, Glut-4 (plasma membrane protein), LXRα, LaminB1 and β-actin (Cell Signaling Technology, Inc., Massachusetts, USA) and anti-mouse adiponectin (Abcam) at 4°C overnight.

    Techniques: Quantitative RT-PCR, Western Blot, Phospho-proteomics, Control, Membrane, Immunofluorescence, Injection, Saline

    A–B, quantitative real-time RT-PCR analyses of adiponectin receptors 1 (AdipoR1) and 2 (AdipoR2) mRNAs in liver (A); Western blotting analyses of phosphorylation of AMPK, phosphorylation of ACC, IRS-1 and PPARα protein levels using β-actin as a loading control in liver (B). All values are presented as means ± SEM, n = 4–6 mice per group. * P <0.05, ** P <0.01 vs. control mice treated with DMSO.

    Journal: PLoS ONE

    Article Title: Regulation of Insulin Resistance and Adiponectin Signaling in Adipose Tissue by Liver X Receptor Activation Highlights a Cross-Talk with PPARγ

    doi: 10.1371/journal.pone.0101269

    Figure Lengend Snippet: A–B, quantitative real-time RT-PCR analyses of adiponectin receptors 1 (AdipoR1) and 2 (AdipoR2) mRNAs in liver (A); Western blotting analyses of phosphorylation of AMPK, phosphorylation of ACC, IRS-1 and PPARα protein levels using β-actin as a loading control in liver (B). All values are presented as means ± SEM, n = 4–6 mice per group. * P <0.05, ** P <0.01 vs. control mice treated with DMSO.

    Article Snippet: Membranes were then incubated with primary antibodies (diluted 1∶1,000) including anti-rabbit p-AMPK, AMPK, p-ACC, ACC, PPARα, IRS-1, Glut-4 (plasma membrane protein), LXRα, LaminB1 and β-actin (Cell Signaling Technology, Inc., Massachusetts, USA) and anti-mouse adiponectin (Abcam) at 4°C overnight.

    Techniques: Quantitative RT-PCR, Western Blot, Phospho-proteomics, Control