glut4 expression  (Cell Signaling Technology Inc)

 
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    Name:
    Glut4 Antibody
    Description:
    A group of related glucose transporters Glut1 5 and 7 mediate the facilitated diffusion of glucose in nonepithelial mammalian tissues Within insulin responsive tissues such as muscle and fat Glut1 contributes to basal glucose uptake while Glut4 is responsible for insulin stimulated glucose transport 1 3 Glut4 is a 12 transmembrane domain protein that facilitates glucose transport in the direction of the glucose gradient This transporter localizes to intracellular organelles endosomes in unstimulated cells and translocates to the cell surface following insulin stimulation 1 2 4 Translocation of Glut4 is dependent on Akt which may act by phosphorylating AS160 a RabGAP protein involved in membrane trafficking 5
    Catalog Number:
    2299
    Price:
    None
    Category:
    Primary Antibodies
    Source:
    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to a sequence of human Glut4 (around Q6). Antibodies are purified by protein A and peptide affinity chromatography.
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    Structured Review

    Cell Signaling Technology Inc glut4 expression
    Inhibition of Kv1.3 stimulates glucose uptake and <t>GLUT4</t> translocation in adipose tissue and skeletal muscle. ( A ) Glucose uptake in adipose tissue. ( Left ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3+/+ mice. ( Right ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3-/- mice. Baseline and insulin-stimulated uptake at 20 min are significantly higher in Kv1.3-/- than in control littermate mice ( n = 5, P
    A group of related glucose transporters Glut1 5 and 7 mediate the facilitated diffusion of glucose in nonepithelial mammalian tissues Within insulin responsive tissues such as muscle and fat Glut1 contributes to basal glucose uptake while Glut4 is responsible for insulin stimulated glucose transport 1 3 Glut4 is a 12 transmembrane domain protein that facilitates glucose transport in the direction of the glucose gradient This transporter localizes to intracellular organelles endosomes in unstimulated cells and translocates to the cell surface following insulin stimulation 1 2 4 Translocation of Glut4 is dependent on Akt which may act by phosphorylating AS160 a RabGAP protein involved in membrane trafficking 5
    https://www.bioz.com/result/glut4 expression/product/Cell Signaling Technology Inc
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    glut4 expression - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity"

    Article Title: The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.0308450100

    Inhibition of Kv1.3 stimulates glucose uptake and GLUT4 translocation in adipose tissue and skeletal muscle. ( A ) Glucose uptake in adipose tissue. ( Left ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3+/+ mice. ( Right ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3-/- mice. Baseline and insulin-stimulated uptake at 20 min are significantly higher in Kv1.3-/- than in control littermate mice ( n = 5, P
    Figure Legend Snippet: Inhibition of Kv1.3 stimulates glucose uptake and GLUT4 translocation in adipose tissue and skeletal muscle. ( A ) Glucose uptake in adipose tissue. ( Left ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3+/+ mice. ( Right ) Baseline and insulin-stimulated glucose uptake in adipose tissue of Kv1.3-/- mice. Baseline and insulin-stimulated uptake at 20 min are significantly higher in Kv1.3-/- than in control littermate mice ( n = 5, P

    Techniques Used: Inhibition, Translocation Assay, Mouse Assay

    2) Product Images from "Regulation of insulin secretion and GLUT4 tra3cking by the calcium sensor synaptotagmin VII ☆"

    Article Title: Regulation of insulin secretion and GLUT4 tra3cking by the calcium sensor synaptotagmin VII ☆

    Journal:

    doi: 10.1016/j.bbrc.2007.08.023

    Dysregulated GLUT4 traffic in Syt VII−/− mice. (A) GLUT4 traffic in WT and Syt VII−/− fat cells: GLUT4 distribution examined by confocal microscopy in adipocytes, isolated from wild-type littermate (WT, n = 3) and Syt VII−/−,
    Figure Legend Snippet: Dysregulated GLUT4 traffic in Syt VII−/− mice. (A) GLUT4 traffic in WT and Syt VII−/− fat cells: GLUT4 distribution examined by confocal microscopy in adipocytes, isolated from wild-type littermate (WT, n = 3) and Syt VII−/−,

    Techniques Used: Mouse Assay, Confocal Microscopy, Isolation

    Colocalization of GLUT4, Syt VII, and Kv1.3. Unstimulated adipocytes isolated from wild-type mice, maintained in primary culture, and examined by confocal microscopy. Colocalization of (A) GLUT4 and Syt VII, (B) Kv1.3 and GLUT4, (C) Kv1.3 and Syt VII.
    Figure Legend Snippet: Colocalization of GLUT4, Syt VII, and Kv1.3. Unstimulated adipocytes isolated from wild-type mice, maintained in primary culture, and examined by confocal microscopy. Colocalization of (A) GLUT4 and Syt VII, (B) Kv1.3 and GLUT4, (C) Kv1.3 and Syt VII.

    Techniques Used: Isolation, Mouse Assay, Confocal Microscopy

    Related Articles

    Microscopy:

    Article Title: Linking cytoarchitecture to metabolism: sarcolemma-associated plectin affects glucose uptake by destabilizing microtubule networks in mdx myofibers
    Article Snippet: .. Antibodies For immunofluorescence microscopy (IFM) and immunoblotting (IB) the following antibodies were used: mAb to α-tubulin (IFM; Acris, Herford, Germany), mAb to desmin (IFM; Dako Cytomation, Glostrup, Denmark), antisera #9 (IB) and #46 (IFM) to plectin [ ], anti-GLUT4 (IFM; a kind gift from Dr. Hadi Al-Hasani, German Diabetes Center, Düsseldorf, Germany; IB; #2299; Cell Signaling, Danvers, MA, USA), anti-sarcomeric α-actinin (IFM; Sigma, St. Louis, MO, USA), anti-dystrophin (IB; NCL-Dys1; Leica Biosystems Newcastle Ltd, Newcastle upon Tyne, UK), anti-α-tubulin (IB; DM1A, Abcam, Cambridge, UK), anti-acetylated tubulin (IB; 6-11-B1; Sigma, St. Louis, MO, USA), anti-tau (IB; A0028; Dako, Glostrup, Denmark), and mAB to HA-tag (GLUT4 translocation assay; HA.11; Covance, Berkeley, CA, USA). .. As secondary antibodies we used donkey anti-rat 633, goat anti-rat Cy5, goat anti-mouse 488, and donkey anti-mouse Dylight 649 for IFM and HRPO-conjugated goat anti-rabbit or goat anti-mouse for IB (all Jackson ImmunoResearch, West Grove, PA, USA).

    Immunofluorescence:

    Article Title: Linking cytoarchitecture to metabolism: sarcolemma-associated plectin affects glucose uptake by destabilizing microtubule networks in mdx myofibers
    Article Snippet: .. Antibodies For immunofluorescence microscopy (IFM) and immunoblotting (IB) the following antibodies were used: mAb to α-tubulin (IFM; Acris, Herford, Germany), mAb to desmin (IFM; Dako Cytomation, Glostrup, Denmark), antisera #9 (IB) and #46 (IFM) to plectin [ ], anti-GLUT4 (IFM; a kind gift from Dr. Hadi Al-Hasani, German Diabetes Center, Düsseldorf, Germany; IB; #2299; Cell Signaling, Danvers, MA, USA), anti-sarcomeric α-actinin (IFM; Sigma, St. Louis, MO, USA), anti-dystrophin (IB; NCL-Dys1; Leica Biosystems Newcastle Ltd, Newcastle upon Tyne, UK), anti-α-tubulin (IB; DM1A, Abcam, Cambridge, UK), anti-acetylated tubulin (IB; 6-11-B1; Sigma, St. Louis, MO, USA), anti-tau (IB; A0028; Dako, Glostrup, Denmark), and mAB to HA-tag (GLUT4 translocation assay; HA.11; Covance, Berkeley, CA, USA). .. As secondary antibodies we used donkey anti-rat 633, goat anti-rat Cy5, goat anti-mouse 488, and donkey anti-mouse Dylight 649 for IFM and HRPO-conjugated goat anti-rabbit or goat anti-mouse for IB (all Jackson ImmunoResearch, West Grove, PA, USA).

    Incubation:

    Article Title: Preoperative Oral Carbohydrate Improved Postoperative Insulin Resistance in Rats through the PI3K/AKT/mTOR Pathway
    Article Snippet: .. Membranes were blocked with 5% milk in Tris Buffered Saline with Tween 20 (TBS-T) and subsequently incubated with primary antibody in TBS-T supplemented with 5% blocking milk in 1: 1000 dilution of rabbit anti-mTOR (#2972S, Cell Signaling, USA) and anti-p-mTOR (Ser2448) (#2971P, Cell Signaling, USA), anti-IRS-1(59G8) (#2390, Cell Signaling, USA) and anti-p-IRS-1 (Ser302) (#2384, Cell Signaling, USA), anti-PI3Kp85 (#4292, Cell Signaling, USA) and anti-p-PI3K p85 (Tyr458) (#4228, Cell Signaling, USA), anti-AKT (4685S, Cell Signaling, USA) and anti-p-AKT(Thr308) (#2965P, Cell Signaling, USA), and anti-GluT4 (#2213S, Cell Signaling, USA) and anti-β-actin (sc-47778, Santa Cruz, USA). .. An IRDye 800CW (926-32210) (LI-COR, USA) was used as a secondary antibody.

    Article Title: Free fatty acid can induce cardiac dysfunction and alter insulin signaling pathways in the heart
    Article Snippet: .. Membranes were blocked with 5% BSA in PBS plus Tween 20 at room temperature for 2 h, and then incubated with anti-PI3K (P110α), anti-Akt (Ser172), anti-phospho-Akt (Ser172), anti-GLUT4, anti-AMPK (Thr172), anti-phospho-AMPK (Thr172), and anti-eNOS antibodies (Cell Signaling Technology, Danvers, MA) at 4 °C overnight. .. Membranes were subsequently washed and incubated with the relevant secondary horseradish peroxidase-conjugated antibodies (1:5000; ZSGB-BIO, Beijing, China) for 90 min. β-actin (mouse anti-β-actin; 1:500; ZSGB-BIO) was used as the loading control.

    Article Title: Anti-diabetic activity of stigmasterol from soybean oil by targeting the GLUT4 glucose transporter
    Article Snippet: .. Then the membranes were blocked with 5% evaporated milk and incubated with primary antibodies GLUT4 and β-Actin (Cell Signaling Technology., Danvers, MA, USA) at 4°C overnight. .. The membranes were washed out for three times with washing buffer, and subsequently incubated with HRP-conjugated secondary antibodies (Cell Signaling Technology, Beverly, MA, USA) for 1 h at room temperature.

    other:

    Article Title: Obestatin as a regulator of adipocyte metabolism and adipogenesis
    Article Snippet: Anti-pAkt HM (S473), anti-pAMPKα(T172), anti-pGSK3α/β(S21/9), anti-pmTOR(S2448), anti-pS6K1(T389), anti-pACC(S79), anti-GLUT4 and anti-tubulin antibodies were from Cell Signaling Technology (MA, USA).

    Blocking Assay:

    Article Title: Preoperative Oral Carbohydrate Improved Postoperative Insulin Resistance in Rats through the PI3K/AKT/mTOR Pathway
    Article Snippet: .. Membranes were blocked with 5% milk in Tris Buffered Saline with Tween 20 (TBS-T) and subsequently incubated with primary antibody in TBS-T supplemented with 5% blocking milk in 1: 1000 dilution of rabbit anti-mTOR (#2972S, Cell Signaling, USA) and anti-p-mTOR (Ser2448) (#2971P, Cell Signaling, USA), anti-IRS-1(59G8) (#2390, Cell Signaling, USA) and anti-p-IRS-1 (Ser302) (#2384, Cell Signaling, USA), anti-PI3Kp85 (#4292, Cell Signaling, USA) and anti-p-PI3K p85 (Tyr458) (#4228, Cell Signaling, USA), anti-AKT (4685S, Cell Signaling, USA) and anti-p-AKT(Thr308) (#2965P, Cell Signaling, USA), and anti-GluT4 (#2213S, Cell Signaling, USA) and anti-β-actin (sc-47778, Santa Cruz, USA). .. An IRDye 800CW (926-32210) (LI-COR, USA) was used as a secondary antibody.

    Translocation Assay:

    Article Title: Linking cytoarchitecture to metabolism: sarcolemma-associated plectin affects glucose uptake by destabilizing microtubule networks in mdx myofibers
    Article Snippet: .. Antibodies For immunofluorescence microscopy (IFM) and immunoblotting (IB) the following antibodies were used: mAb to α-tubulin (IFM; Acris, Herford, Germany), mAb to desmin (IFM; Dako Cytomation, Glostrup, Denmark), antisera #9 (IB) and #46 (IFM) to plectin [ ], anti-GLUT4 (IFM; a kind gift from Dr. Hadi Al-Hasani, German Diabetes Center, Düsseldorf, Germany; IB; #2299; Cell Signaling, Danvers, MA, USA), anti-sarcomeric α-actinin (IFM; Sigma, St. Louis, MO, USA), anti-dystrophin (IB; NCL-Dys1; Leica Biosystems Newcastle Ltd, Newcastle upon Tyne, UK), anti-α-tubulin (IB; DM1A, Abcam, Cambridge, UK), anti-acetylated tubulin (IB; 6-11-B1; Sigma, St. Louis, MO, USA), anti-tau (IB; A0028; Dako, Glostrup, Denmark), and mAB to HA-tag (GLUT4 translocation assay; HA.11; Covance, Berkeley, CA, USA). .. As secondary antibodies we used donkey anti-rat 633, goat anti-rat Cy5, goat anti-mouse 488, and donkey anti-mouse Dylight 649 for IFM and HRPO-conjugated goat anti-rabbit or goat anti-mouse for IB (all Jackson ImmunoResearch, West Grove, PA, USA).

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  • 94
    Cell Signaling Technology Inc glut4
    Effects of green coffee bean extract and 5-CQA supplementation on the proteins involved in <t>GLUT4</t> translocation in mice fed a HFD. Protein levels of p-IRS1, p-AKT, plasma membrane GLUT4, and corresponding total proteins in the epididymal adipose tissue were determined by Western blotting. Data represent the results of three independent experiments ( n = 2, 3 mice per experiment). P
    Glut4, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 148 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glut4/product/Cell Signaling Technology Inc
    Average 94 stars, based on 148 article reviews
    Price from $9.99 to $1999.99
    glut4 - by Bioz Stars, 2020-09
    94/100 stars
      Buy from Supplier

    Image Search Results


    Effects of green coffee bean extract and 5-CQA supplementation on the proteins involved in GLUT4 translocation in mice fed a HFD. Protein levels of p-IRS1, p-AKT, plasma membrane GLUT4, and corresponding total proteins in the epididymal adipose tissue were determined by Western blotting. Data represent the results of three independent experiments ( n = 2, 3 mice per experiment). P

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Decaffeinated Green Coffee Bean Extract Attenuates Diet-Induced Obesity and Insulin Resistance in Mice

    doi: 10.1155/2014/718379

    Figure Lengend Snippet: Effects of green coffee bean extract and 5-CQA supplementation on the proteins involved in GLUT4 translocation in mice fed a HFD. Protein levels of p-IRS1, p-AKT, plasma membrane GLUT4, and corresponding total proteins in the epididymal adipose tissue were determined by Western blotting. Data represent the results of three independent experiments ( n = 2, 3 mice per experiment). P

    Article Snippet: Mice fed the green coffee bean extract exhibited increased phosphorylation of AKT and translocation of GLUT4 from the cytosol to the membrane when compared with those fed a HFD.

    Techniques: Translocation Assay, Mouse Assay, Western Blot

    The possible molecular mechanisms of decaffeinated green coffee bean extract in attenuating adipogenesis, inflammation, and insulin resistance induced by HFD. Decaffeinated green coffee bean extract reverses HFD-induced changes in expression of genes involved in WNT10b- and galanin-mediated adipogenesis cascades in the epididymal adipose tissue. The downstream adipogenic transcription factors (PPAR γ 2 and C/EBP α ) and their target genes were also suppressed by decaffeinated green coffee bean extract in the epididymal adipose tissue. Decaffeinated green coffee bean extract reverses the HFD-induced changes in the expression of genes related to TLR2/4-mediated proinflammatory signaling cascades and proteins involved in GLUT4 translocation in the epididymal adipose tissue.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Decaffeinated Green Coffee Bean Extract Attenuates Diet-Induced Obesity and Insulin Resistance in Mice

    doi: 10.1155/2014/718379

    Figure Lengend Snippet: The possible molecular mechanisms of decaffeinated green coffee bean extract in attenuating adipogenesis, inflammation, and insulin resistance induced by HFD. Decaffeinated green coffee bean extract reverses HFD-induced changes in expression of genes involved in WNT10b- and galanin-mediated adipogenesis cascades in the epididymal adipose tissue. The downstream adipogenic transcription factors (PPAR γ 2 and C/EBP α ) and their target genes were also suppressed by decaffeinated green coffee bean extract in the epididymal adipose tissue. Decaffeinated green coffee bean extract reverses the HFD-induced changes in the expression of genes related to TLR2/4-mediated proinflammatory signaling cascades and proteins involved in GLUT4 translocation in the epididymal adipose tissue.

    Article Snippet: Mice fed the green coffee bean extract exhibited increased phosphorylation of AKT and translocation of GLUT4 from the cytosol to the membrane when compared with those fed a HFD.

    Techniques: Expressing, Translocation Assay

    Schematic representation of the different steps leading to glucose uptake due to depletion of RIP140 in oxidative muscle. Absence of RIP140 leads to expression of UCP1 and mitochondrial uncoupling. Then, alteration of the AMP to ATP ratio in favor of elevated AMP activates AMPK which in turn stimulates GLUT4 translocation to the plasma membrane enabling the entry of glucose from blood circulation.

    Journal: PLoS ONE

    Article Title: Absence of RIP140 Reveals a Pathway Regulating glut4-Dependent Glucose Uptake in Oxidative Skeletal Muscle through UCP1-Mediated Activation of AMPK

    doi: 10.1371/journal.pone.0032520

    Figure Lengend Snippet: Schematic representation of the different steps leading to glucose uptake due to depletion of RIP140 in oxidative muscle. Absence of RIP140 leads to expression of UCP1 and mitochondrial uncoupling. Then, alteration of the AMP to ATP ratio in favor of elevated AMP activates AMPK which in turn stimulates GLUT4 translocation to the plasma membrane enabling the entry of glucose from blood circulation.

    Article Snippet: Analysis of GLUT4 and tubulin expression in RIP140 transgenic (TG) and WT EDL by western blot. (TIF) Click here for additional data file.

    Techniques: Expressing, Translocation Assay

    Depletion of RIP140 increases the presence of GLUT4 at the plasma membrane and basal glucose uptake in the soleus. (A) Basal glucose uptake, normalized to proteins, monitored in EDL (n = 4) and soleus (SOL) (n = 8) isolated from RIP140 transgenic (TG) and WT mice. Data are expressed as mean ± SEM. *p

    Journal: PLoS ONE

    Article Title: Absence of RIP140 Reveals a Pathway Regulating glut4-Dependent Glucose Uptake in Oxidative Skeletal Muscle through UCP1-Mediated Activation of AMPK

    doi: 10.1371/journal.pone.0032520

    Figure Lengend Snippet: Depletion of RIP140 increases the presence of GLUT4 at the plasma membrane and basal glucose uptake in the soleus. (A) Basal glucose uptake, normalized to proteins, monitored in EDL (n = 4) and soleus (SOL) (n = 8) isolated from RIP140 transgenic (TG) and WT mice. Data are expressed as mean ± SEM. *p

    Article Snippet: Analysis of GLUT4 and tubulin expression in RIP140 transgenic (TG) and WT EDL by western blot. (TIF) Click here for additional data file.

    Techniques: Isolation, Transgenic Assay, Mouse Assay

    TUSC5 promotes intracellular associations during protein recycling . ( A ) Western blot of immunoprecipitation of endogenous cellugyrin (CG) from 3T3-L1 adipocytes after siRNA-mediated TUSC5 knockdown. ( B ) Western blot of immunoprecipitation of endogenous GLUT4 from 3T3-L1 adipocytes in control and TUSC5 knockdown conditions. ( C ) MS1 intensities from mass spectrometric analysis of co-precipitants of GLUT4 IPs as in 2D (n = 4). *p

    Journal: Molecular Metabolism

    Article Title: TUSC5 regulates insulin-mediated adipose tissue glucose uptake by modulation of GLUT4 recycling

    doi: 10.1016/j.molmet.2015.08.003

    Figure Lengend Snippet: TUSC5 promotes intracellular associations during protein recycling . ( A ) Western blot of immunoprecipitation of endogenous cellugyrin (CG) from 3T3-L1 adipocytes after siRNA-mediated TUSC5 knockdown. ( B ) Western blot of immunoprecipitation of endogenous GLUT4 from 3T3-L1 adipocytes in control and TUSC5 knockdown conditions. ( C ) MS1 intensities from mass spectrometric analysis of co-precipitants of GLUT4 IPs as in 2D (n = 4). *p

    Article Snippet: Expression levels of GLUT4 and AKT, as well as phosphorylation of AKT (pAKT), were not affected by TUSC5 knockdown, in vitro or in vivo ( , data not shown), demonstrating that post-receptor insulin signaling is not dependent on TUSC5.

    Techniques: Western Blot, Immunoprecipitation

    TUSC5 co-localizes with GLUT4 . ( A ) Representative immuno-fluorescence images of whole tissue mounts of eWAT from fasted wild-type and Tusc5 knockout C57Bl/6 mice for TUSC5 and GLUT4 (scale: 100 μm). ( B ) Representative immunofluorescence images of TUSC5 and GLUT4 staining in 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (100 nM) (scale: 50 μm) at different time points. ( C ) Western blot on low-density microsome (LDM) and plasma membrane fractions from 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (100 nM) for GLUT4 and TUSC5.

    Journal: Molecular Metabolism

    Article Title: TUSC5 regulates insulin-mediated adipose tissue glucose uptake by modulation of GLUT4 recycling

    doi: 10.1016/j.molmet.2015.08.003

    Figure Lengend Snippet: TUSC5 co-localizes with GLUT4 . ( A ) Representative immuno-fluorescence images of whole tissue mounts of eWAT from fasted wild-type and Tusc5 knockout C57Bl/6 mice for TUSC5 and GLUT4 (scale: 100 μm). ( B ) Representative immunofluorescence images of TUSC5 and GLUT4 staining in 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (100 nM) (scale: 50 μm) at different time points. ( C ) Western blot on low-density microsome (LDM) and plasma membrane fractions from 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (100 nM) for GLUT4 and TUSC5.

    Article Snippet: Expression levels of GLUT4 and AKT, as well as phosphorylation of AKT (pAKT), were not affected by TUSC5 knockdown, in vitro or in vivo ( , data not shown), demonstrating that post-receptor insulin signaling is not dependent on TUSC5.

    Techniques: Fluorescence, Knock-Out, Mouse Assay, Immunofluorescence, Staining, Western Blot

    TUSC5 interacts with GLUT4 and is involved in insulin-stimulated GLUT4 trafficking . ( A ) Western blot of immunoprecipitation of endogenous TUSC5 from 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (10 nM). ( B ) Mass spectrometric identification of co-precipitants from TUSC5 and GLUT4 IPs (n = 4). *p

    Journal: Molecular Metabolism

    Article Title: TUSC5 regulates insulin-mediated adipose tissue glucose uptake by modulation of GLUT4 recycling

    doi: 10.1016/j.molmet.2015.08.003

    Figure Lengend Snippet: TUSC5 interacts with GLUT4 and is involved in insulin-stimulated GLUT4 trafficking . ( A ) Western blot of immunoprecipitation of endogenous TUSC5 from 3T3-L1 adipocytes in basal (0 nM) and insulin-stimulated state (10 nM). ( B ) Mass spectrometric identification of co-precipitants from TUSC5 and GLUT4 IPs (n = 4). *p

    Article Snippet: Expression levels of GLUT4 and AKT, as well as phosphorylation of AKT (pAKT), were not affected by TUSC5 knockdown, in vitro or in vivo ( , data not shown), demonstrating that post-receptor insulin signaling is not dependent on TUSC5.

    Techniques: Western Blot, Immunoprecipitation

    TUSC5 is adipocyte specifically expressed and is important for insulin-stimulated glucose uptake . ( A – C ) qRT-PCR for Tusc5 ( A ), Glut4 ( B ) and sortilin ( C ) mRNA expression in various wild-type C57Bl/6 mouse tissues (n = 5). ( D ) Insulin-stimulated and basal uptake of 2-deoxyglucose in 3T3-L1 adipocytes after shRNA-mediated TUSC5 knockdown (n = 3). ( E ) Insulin-stimulated and basal uptake of 2-deoxyglucose in eWAT of wild-type C57Bl/6 mice 6 days after shRNA-mediated TUSC5 knockdown (n = 6–10).

    Journal: Molecular Metabolism

    Article Title: TUSC5 regulates insulin-mediated adipose tissue glucose uptake by modulation of GLUT4 recycling

    doi: 10.1016/j.molmet.2015.08.003

    Figure Lengend Snippet: TUSC5 is adipocyte specifically expressed and is important for insulin-stimulated glucose uptake . ( A – C ) qRT-PCR for Tusc5 ( A ), Glut4 ( B ) and sortilin ( C ) mRNA expression in various wild-type C57Bl/6 mouse tissues (n = 5). ( D ) Insulin-stimulated and basal uptake of 2-deoxyglucose in 3T3-L1 adipocytes after shRNA-mediated TUSC5 knockdown (n = 3). ( E ) Insulin-stimulated and basal uptake of 2-deoxyglucose in eWAT of wild-type C57Bl/6 mice 6 days after shRNA-mediated TUSC5 knockdown (n = 6–10).

    Article Snippet: Expression levels of GLUT4 and AKT, as well as phosphorylation of AKT (pAKT), were not affected by TUSC5 knockdown, in vitro or in vivo ( , data not shown), demonstrating that post-receptor insulin signaling is not dependent on TUSC5.

    Techniques: Quantitative RT-PCR, Expressing, shRNA, Mouse Assay