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anti glut1 primary antibody  (Proteintech)


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    Structured Review

    Proteintech anti glut1 primary antibody
    <t>GLUT1</t> is elevated in the nasal mucosa and positively correlated with disease severity in AR patients. (A–B) Immunofluorescence staining for GLUT1 (n = 12); (C–D) WB showing GLUT1 protein expression (n = 12); (E) RT-qPCR for GLUT1 (n = 30); (F–G) The correlations between GLUT1 mRNA, VAS and TNSS in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, <t>glucose</t> <t>transporter</t> 1; WB, western blotting; RT-qPCR, quantitative reverse transcription polymerase chain reaction; VAS, visual analog scale; TNSS, total nasal symptom score. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.
    Anti Glut1 Primary Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 450 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti glut1 primary antibody/product/Proteintech
    Average 96 stars, based on 450 article reviews
    anti glut1 primary antibody - by Bioz Stars, 2026-03
    96/100 stars

    Images

    1) Product Images from "Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis "

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    Journal: The World Allergy Organization Journal

    doi: 10.1016/j.waojou.2025.101158

    GLUT1 is elevated in the nasal mucosa and positively correlated with disease severity in AR patients. (A–B) Immunofluorescence staining for GLUT1 (n = 12); (C–D) WB showing GLUT1 protein expression (n = 12); (E) RT-qPCR for GLUT1 (n = 30); (F–G) The correlations between GLUT1 mRNA, VAS and TNSS in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; WB, western blotting; RT-qPCR, quantitative reverse transcription polymerase chain reaction; VAS, visual analog scale; TNSS, total nasal symptom score. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.
    Figure Legend Snippet: GLUT1 is elevated in the nasal mucosa and positively correlated with disease severity in AR patients. (A–B) Immunofluorescence staining for GLUT1 (n = 12); (C–D) WB showing GLUT1 protein expression (n = 12); (E) RT-qPCR for GLUT1 (n = 30); (F–G) The correlations between GLUT1 mRNA, VAS and TNSS in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; WB, western blotting; RT-qPCR, quantitative reverse transcription polymerase chain reaction; VAS, visual analog scale; TNSS, total nasal symptom score. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Techniques Used: Immunofluorescence, Staining, Expressing, Quantitative RT-PCR, Control, Western Blot, Reverse Transcription, Polymerase Chain Reaction

    Increased GLUT1 is associated with epithelial tight junction marker expression in AR patients. (A–B) Tissue multiplex immunofluorescence for GLUT1, ZO-1, and occluding; (C–D) RT-qPCR for ZO-1 and occluding between the 2 groups (n = 30); (E–F) The correlations between GLUT1 mRNA, ZO-1 and occluding mRNA in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; RT-qPCR, quantitative reverse transcription polymerase chain reaction. ∗∗P < 0.01, ∗∗∗P < 0.001.
    Figure Legend Snippet: Increased GLUT1 is associated with epithelial tight junction marker expression in AR patients. (A–B) Tissue multiplex immunofluorescence for GLUT1, ZO-1, and occluding; (C–D) RT-qPCR for ZO-1 and occluding between the 2 groups (n = 30); (E–F) The correlations between GLUT1 mRNA, ZO-1 and occluding mRNA in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; RT-qPCR, quantitative reverse transcription polymerase chain reaction. ∗∗P < 0.01, ∗∗∗P < 0.001.

    Techniques Used: Marker, Expressing, Multiplex Assay, Immunofluorescence, Quantitative RT-PCR, Control, Reverse Transcription, Polymerase Chain Reaction

    HDM stimulation promotes GLUT1 expression and inhibits tight junction marker expression in nasal epithelial cells. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with different concentrations of HDM (n = 6); (C–D) WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells treated with different concentrations of HDM (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.
    Figure Legend Snippet: HDM stimulation promotes GLUT1 expression and inhibits tight junction marker expression in nasal epithelial cells. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with different concentrations of HDM (n = 6); (C–D) WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells treated with different concentrations of HDM (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Techniques Used: Expressing, Marker, Immunofluorescence, Staining, Western Blot

    Inhibiting GLUT1 alleviates the suppression of tight junction marker expression in nasal epithelial cells mediated by HDM. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with PBS, HDM and HDM + BAY876 (n = 6); WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells among the 3 groups (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.
    Figure Legend Snippet: Inhibiting GLUT1 alleviates the suppression of tight junction marker expression in nasal epithelial cells mediated by HDM. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with PBS, HDM and HDM + BAY876 (n = 6); WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells among the 3 groups (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Techniques Used: Marker, Expressing, Immunofluorescence, Staining, Western Blot

    GLUT1 inhibitor alleviates allergen-mediated nasal mucosal inflammation and barrier function damage in murine AR model. (A) Representative HE and immunofluorescence images of nasal mucosal in PBS, AR and AR + BAY876 groups (n = 5); (B) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (C) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (D) IL-4, IL-13, IL-17A and IFN-γ concentrations in nasal lavage fluid (n = 5). AR, allergic rhinitis; GLUT1, glucose transporter 1; ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.
    Figure Legend Snippet: GLUT1 inhibitor alleviates allergen-mediated nasal mucosal inflammation and barrier function damage in murine AR model. (A) Representative HE and immunofluorescence images of nasal mucosal in PBS, AR and AR + BAY876 groups (n = 5); (B) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (C) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (D) IL-4, IL-13, IL-17A and IFN-γ concentrations in nasal lavage fluid (n = 5). AR, allergic rhinitis; GLUT1, glucose transporter 1; ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Techniques Used: Immunofluorescence, Fluorescence



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    Article Title: Chromium picolinate alleviates heat stress-induced breast muscle glucose and lipid metabolism disorders in broiler chickens

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    Figure Lengend Snippet: Effects of chromium picolinate on breast muscle glycolipid metabolism genes expression of broilers under heat stress. (A) Western blot analysis. (B) GLUT1. (C) PI3K. (D) GS. (E) PPARα. (F) CPT-1. (G) LPL. Abbreviation: GLUT1: glucose transporter 1, PI3K: phosphatidylinositol 3 kinase, GS: glycogen synthase, PPARα: peroxisome proliferators-activated receptors α, CPT-1; carnitine palmitoyl transterase-1, LPL: lipoprotein lipase. In the same rank, a, b, c values with different small letter superscripts mean significant difference ( P < 0.05).

    Article Snippet: Primary antibodies against GLUT1 (1:1000, AWA61570 , Abiowell), PI3K (1:1000, AWA63394 , Abiowell), GS (1:1000, AWA43660 , Abiowell), CPT1 (1:1000, AWA63836 , Abiowell), LPL (1:1000, AWA61104 , Abiowell), PPARα (1:500, BS-23398, BIOSS) and β-actin (1:2000, AWA80002 ; Abiowell) were diluted in antibody diluent (AWB0200c; Abiowell) and incubated with the membrane overnight at 4°C.

    Techniques: Expressing, Western Blot

    GLUT1 is elevated in the nasal mucosa and positively correlated with disease severity in AR patients. (A–B) Immunofluorescence staining for GLUT1 (n = 12); (C–D) WB showing GLUT1 protein expression (n = 12); (E) RT-qPCR for GLUT1 (n = 30); (F–G) The correlations between GLUT1 mRNA, VAS and TNSS in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; WB, western blotting; RT-qPCR, quantitative reverse transcription polymerase chain reaction; VAS, visual analog scale; TNSS, total nasal symptom score. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Journal: The World Allergy Organization Journal

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    doi: 10.1016/j.waojou.2025.101158

    Figure Lengend Snippet: GLUT1 is elevated in the nasal mucosa and positively correlated with disease severity in AR patients. (A–B) Immunofluorescence staining for GLUT1 (n = 12); (C–D) WB showing GLUT1 protein expression (n = 12); (E) RT-qPCR for GLUT1 (n = 30); (F–G) The correlations between GLUT1 mRNA, VAS and TNSS in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; WB, western blotting; RT-qPCR, quantitative reverse transcription polymerase chain reaction; VAS, visual analog scale; TNSS, total nasal symptom score. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Article Snippet: Slides were then incubated overnight at 4 °C with an anti-GLUT1 primary antibody (1:200, Proteintech, Wuhan, China).

    Techniques: Immunofluorescence, Staining, Expressing, Quantitative RT-PCR, Control, Western Blot, Reverse Transcription, Polymerase Chain Reaction

    Increased GLUT1 is associated with epithelial tight junction marker expression in AR patients. (A–B) Tissue multiplex immunofluorescence for GLUT1, ZO-1, and occluding; (C–D) RT-qPCR for ZO-1 and occluding between the 2 groups (n = 30); (E–F) The correlations between GLUT1 mRNA, ZO-1 and occluding mRNA in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; RT-qPCR, quantitative reverse transcription polymerase chain reaction. ∗∗P < 0.01, ∗∗∗P < 0.001.

    Journal: The World Allergy Organization Journal

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    doi: 10.1016/j.waojou.2025.101158

    Figure Lengend Snippet: Increased GLUT1 is associated with epithelial tight junction marker expression in AR patients. (A–B) Tissue multiplex immunofluorescence for GLUT1, ZO-1, and occluding; (C–D) RT-qPCR for ZO-1 and occluding between the 2 groups (n = 30); (E–F) The correlations between GLUT1 mRNA, ZO-1 and occluding mRNA in AR patients (n = 30). AR, allergic rhinitis; HCs, healthy control; GLUT1, glucose transporter 1; RT-qPCR, quantitative reverse transcription polymerase chain reaction. ∗∗P < 0.01, ∗∗∗P < 0.001.

    Article Snippet: Slides were then incubated overnight at 4 °C with an anti-GLUT1 primary antibody (1:200, Proteintech, Wuhan, China).

    Techniques: Marker, Expressing, Multiplex Assay, Immunofluorescence, Quantitative RT-PCR, Control, Reverse Transcription, Polymerase Chain Reaction

    HDM stimulation promotes GLUT1 expression and inhibits tight junction marker expression in nasal epithelial cells. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with different concentrations of HDM (n = 6); (C–D) WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells treated with different concentrations of HDM (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Journal: The World Allergy Organization Journal

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    doi: 10.1016/j.waojou.2025.101158

    Figure Lengend Snippet: HDM stimulation promotes GLUT1 expression and inhibits tight junction marker expression in nasal epithelial cells. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with different concentrations of HDM (n = 6); (C–D) WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells treated with different concentrations of HDM (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Article Snippet: Slides were then incubated overnight at 4 °C with an anti-GLUT1 primary antibody (1:200, Proteintech, Wuhan, China).

    Techniques: Expressing, Marker, Immunofluorescence, Staining, Western Blot

    Inhibiting GLUT1 alleviates the suppression of tight junction marker expression in nasal epithelial cells mediated by HDM. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with PBS, HDM and HDM + BAY876 (n = 6); WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells among the 3 groups (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Journal: The World Allergy Organization Journal

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    doi: 10.1016/j.waojou.2025.101158

    Figure Lengend Snippet: Inhibiting GLUT1 alleviates the suppression of tight junction marker expression in nasal epithelial cells mediated by HDM. (A–B) Cell immunofluorescence staining for GLUT1, ZO-1 and occluding in nasal epithelial cells treated with PBS, HDM and HDM + BAY876 (n = 6); WB showing GLUT1, ZO-1 and occluding protein expression in nasal epithelial cells among the 3 groups (n = 6). HDM, house dust mite; GLUT1, glucose transporter 1; WB, western blotting. ∗P < 0.05, ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001.

    Article Snippet: Slides were then incubated overnight at 4 °C with an anti-GLUT1 primary antibody (1:200, Proteintech, Wuhan, China).

    Techniques: Marker, Expressing, Immunofluorescence, Staining, Western Blot

    GLUT1 inhibitor alleviates allergen-mediated nasal mucosal inflammation and barrier function damage in murine AR model. (A) Representative HE and immunofluorescence images of nasal mucosal in PBS, AR and AR + BAY876 groups (n = 5); (B) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (C) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (D) IL-4, IL-13, IL-17A and IFN-γ concentrations in nasal lavage fluid (n = 5). AR, allergic rhinitis; GLUT1, glucose transporter 1; ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Journal: The World Allergy Organization Journal

    Article Title: Increased glucose transporter 1 contributes to epithelial barrier dysfunction in allergic rhinitis

    doi: 10.1016/j.waojou.2025.101158

    Figure Lengend Snippet: GLUT1 inhibitor alleviates allergen-mediated nasal mucosal inflammation and barrier function damage in murine AR model. (A) Representative HE and immunofluorescence images of nasal mucosal in PBS, AR and AR + BAY876 groups (n = 5); (B) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (C) Relative fluorescence intensity of GLUT1, ZO-1 and occluding among the 3 groups (n = 5); (D) IL-4, IL-13, IL-17A and IFN-γ concentrations in nasal lavage fluid (n = 5). AR, allergic rhinitis; GLUT1, glucose transporter 1; ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Article Snippet: Slides were then incubated overnight at 4 °C with an anti-GLUT1 primary antibody (1:200, Proteintech, Wuhan, China).

    Techniques: Immunofluorescence, Fluorescence

    Representation of neuropathology evaluation. Brains were collected, post-fixed in 4% paraformaldehyde, blocked, sectioned, and stained by Neuroscience Associates (Knoxville, TN). Neuropathology was evaluated by investigating Glut1 staining to evaluate microvascular density, Immunoglobulin G (IgG) staining to assess blood-brain barrier permeability, and iba-1 staining to investigate neuroinflammation in three regions of interest within the hippocampus (dentate gyrus, cornu ammonis 1, and cornu ammonis 3). Created with BioRender.com .

    Journal: Frontiers in Physiology

    Article Title: Cerebral microvascular density, blood-brain barrier permeability, and support for neuroinflammation indicate early aging in a Marfan syndrome mouse model

    doi: 10.3389/fphys.2024.1457034

    Figure Lengend Snippet: Representation of neuropathology evaluation. Brains were collected, post-fixed in 4% paraformaldehyde, blocked, sectioned, and stained by Neuroscience Associates (Knoxville, TN). Neuropathology was evaluated by investigating Glut1 staining to evaluate microvascular density, Immunoglobulin G (IgG) staining to assess blood-brain barrier permeability, and iba-1 staining to investigate neuroinflammation in three regions of interest within the hippocampus (dentate gyrus, cornu ammonis 1, and cornu ammonis 3). Created with BioRender.com .

    Article Snippet: Glut1, a blood-brain barrier marker, was detected using a rabbit anti-Glut1 primary antibody (Millipore, Catalog# 07-1401; dilution 1:100,000) and a biotinylated goat anti-rabbit IgG secondary antibody (Vector, Catalog# BA-1000; dilution 1:1,000), then visualized using NiDAB as the chromogen.

    Techniques: Staining, Permeability

    Glut1 staining in the Dentate Gyrus (DG) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the DG of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS DG compared to 6M- CTRL, indicative of decreased microvascular density. 6M-MFS compared to 12M-CTRL mice demonstrate no significant differences in Glut1 staining. Male mice are represented with blue data points and females are represented with red data points.

    Journal: Frontiers in Physiology

    Article Title: Cerebral microvascular density, blood-brain barrier permeability, and support for neuroinflammation indicate early aging in a Marfan syndrome mouse model

    doi: 10.3389/fphys.2024.1457034

    Figure Lengend Snippet: Glut1 staining in the Dentate Gyrus (DG) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the DG of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS DG compared to 6M- CTRL, indicative of decreased microvascular density. 6M-MFS compared to 12M-CTRL mice demonstrate no significant differences in Glut1 staining. Male mice are represented with blue data points and females are represented with red data points.

    Article Snippet: Glut1, a blood-brain barrier marker, was detected using a rabbit anti-Glut1 primary antibody (Millipore, Catalog# 07-1401; dilution 1:100,000) and a biotinylated goat anti-rabbit IgG secondary antibody (Vector, Catalog# BA-1000; dilution 1:1,000), then visualized using NiDAB as the chromogen.

    Techniques: Staining

    Glut1 staining in the cornu ammonis 1 (CA1) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the CA1 of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS CA1 compared to 6M-CTRL. 12M-CTRL CA1 demonstrate decreased Glut1 staining compared to 6M-CTRL, with no differences compared to 6M-MFS mice. Male mice are represented with blue data points and females are represented with red data points.

    Journal: Frontiers in Physiology

    Article Title: Cerebral microvascular density, blood-brain barrier permeability, and support for neuroinflammation indicate early aging in a Marfan syndrome mouse model

    doi: 10.3389/fphys.2024.1457034

    Figure Lengend Snippet: Glut1 staining in the cornu ammonis 1 (CA1) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the CA1 of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS CA1 compared to 6M-CTRL. 12M-CTRL CA1 demonstrate decreased Glut1 staining compared to 6M-CTRL, with no differences compared to 6M-MFS mice. Male mice are represented with blue data points and females are represented with red data points.

    Article Snippet: Glut1, a blood-brain barrier marker, was detected using a rabbit anti-Glut1 primary antibody (Millipore, Catalog# 07-1401; dilution 1:100,000) and a biotinylated goat anti-rabbit IgG secondary antibody (Vector, Catalog# BA-1000; dilution 1:1,000), then visualized using NiDAB as the chromogen.

    Techniques: Staining

    Glut1 staining in the cornu ammonis 3 (CA3) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the CA3 of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS CA3 compared to 6M-CTRL. 12M-CTRL CA3 demonstrate decreased Glut1 staining compared to 6M-CTRL, with no differences compared to 6M-MFS mice. Male mice are represented with blue data points and females are represented with red data points.

    Journal: Frontiers in Physiology

    Article Title: Cerebral microvascular density, blood-brain barrier permeability, and support for neuroinflammation indicate early aging in a Marfan syndrome mouse model

    doi: 10.3389/fphys.2024.1457034

    Figure Lengend Snippet: Glut1 staining in the cornu ammonis 3 (CA3) is decreased as a function of genotype and age, indicative of decreased microvascular density. (A) Representative images of Glut1 staining in the CA3 of the hippocampus in 6M-CTRL, 6M-MFS, and 12M-CTRL respectively. Examples of positive signals are represented by white arrows. (B) Glut1 staining is decreased in 6M-MFS CA3 compared to 6M-CTRL. 12M-CTRL CA3 demonstrate decreased Glut1 staining compared to 6M-CTRL, with no differences compared to 6M-MFS mice. Male mice are represented with blue data points and females are represented with red data points.

    Article Snippet: Glut1, a blood-brain barrier marker, was detected using a rabbit anti-Glut1 primary antibody (Millipore, Catalog# 07-1401; dilution 1:100,000) and a biotinylated goat anti-rabbit IgG secondary antibody (Vector, Catalog# BA-1000; dilution 1:1,000), then visualized using NiDAB as the chromogen.

    Techniques: Staining

    Fig. 2. Hypoxia increases interactions between proteins involved in glucose metabolism. (A–C) Volcano plots representing fold enrichment (LFQ intensity) of proteins identified in PFKP IP following exposure of cells to 1% O2 for 8 h (A), 24 h (B), or 48 h (C) relative to normoxic PFKP IP. Proteins involved in glucose metabolism indicated in green. (D) Representative immunoblots reflecting HK2 and PFKP expression following co-IP of GLUT1 from whole cell lysates of Caco-2 cells exposed to 21%/1% O2 for 8 to 48 h (Input = 5% total IP).

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

    Article Title: Hypoxia induces a glycolytic complex in intestinal epithelial cells independent of HIF-1-driven glycolytic gene expression.

    doi: 10.1073/pnas.2208117120

    Figure Lengend Snippet: Fig. 2. Hypoxia increases interactions between proteins involved in glucose metabolism. (A–C) Volcano plots representing fold enrichment (LFQ intensity) of proteins identified in PFKP IP following exposure of cells to 1% O2 for 8 h (A), 24 h (B), or 48 h (C) relative to normoxic PFKP IP. Proteins involved in glucose metabolism indicated in green. (D) Representative immunoblots reflecting HK2 and PFKP expression following co-IP of GLUT1 from whole cell lysates of Caco-2 cells exposed to 21%/1% O2 for 8 to 48 h (Input = 5% total IP).

    Article Snippet: Primary antibodies against GLUT1 (CST #12939, 1:1,000 or Invitrogen MA5- 11315, 1:500), HK2 (Invitrogen MA5- 15679, 1:1,000), PFKP (CST #8164, 1:1,000) HIF- 1α (CST #36169, 1:500 or BD Biosciences #610958, 1:500), Nrf2 (CST #12721, 1:1,000), G6PD (Proteintech 25413- 1- AP, 1: 1,000), MTHFD2 (CST #98116, 1:1,000), β- actin (Sigma A5441, 1:5,000) were used alongside speciesspecific HRP- conjugated secondary antibodies [CST #7074 (Anti- Rabbit IgG), #7076 (Anti- Mouse IgG)].

    Techniques: Western Blot, Expressing, Co-Immunoprecipitation Assay

    Fig. 6. Hypoxia increases interactions between cytosolic HIF-1α and proteins involved in glucose metabolism. (A–C) Volcano plots representing fold enrichment (LFQ intensity) of proteins identified in cytosolic HIF-1α IP following exposure of cells to 1% O2 for 8 h (A), 24 h (B), or 48 h (C) relative to normoxic HIF-1α IP (21% O2). Blue, Proteins understood to interact with HIF-1α. Purple, Proteins involved in glucose metabolism (D and E) Representative immunoblots reflecting GLUT1, PFKP, and HIF-1α expression following co-IP of HIF-1α (D) or GLUT1 (E) from cytosolic hypoxic/normoxic wild-type Caco-2 cell fractions or (F) cytosolic HIF-1A NT Caco-2 cell fractions. (G) Cytosolic inputs for (F). Inputs = 10% IP for (D–G).

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

    Article Title: Hypoxia induces a glycolytic complex in intestinal epithelial cells independent of HIF-1-driven glycolytic gene expression.

    doi: 10.1073/pnas.2208117120

    Figure Lengend Snippet: Fig. 6. Hypoxia increases interactions between cytosolic HIF-1α and proteins involved in glucose metabolism. (A–C) Volcano plots representing fold enrichment (LFQ intensity) of proteins identified in cytosolic HIF-1α IP following exposure of cells to 1% O2 for 8 h (A), 24 h (B), or 48 h (C) relative to normoxic HIF-1α IP (21% O2). Blue, Proteins understood to interact with HIF-1α. Purple, Proteins involved in glucose metabolism (D and E) Representative immunoblots reflecting GLUT1, PFKP, and HIF-1α expression following co-IP of HIF-1α (D) or GLUT1 (E) from cytosolic hypoxic/normoxic wild-type Caco-2 cell fractions or (F) cytosolic HIF-1A NT Caco-2 cell fractions. (G) Cytosolic inputs for (F). Inputs = 10% IP for (D–G).

    Article Snippet: Primary antibodies against GLUT1 (CST #12939, 1:1,000 or Invitrogen MA5- 11315, 1:500), HK2 (Invitrogen MA5- 15679, 1:1,000), PFKP (CST #8164, 1:1,000) HIF- 1α (CST #36169, 1:500 or BD Biosciences #610958, 1:500), Nrf2 (CST #12721, 1:1,000), G6PD (Proteintech 25413- 1- AP, 1: 1,000), MTHFD2 (CST #98116, 1:1,000), β- actin (Sigma A5441, 1:5,000) were used alongside speciesspecific HRP- conjugated secondary antibodies [CST #7074 (Anti- Rabbit IgG), #7076 (Anti- Mouse IgG)].

    Techniques: Western Blot, Expressing, Co-Immunoprecipitation Assay