- PA1-46152 - Invitrogen Antibodies SLC2A1 antibody

Submitted references Synthetic adiponectin-receptor agonist, AdipoRon, induces glycolytic dependence in pancreatic cancer cells.

Manley SJ, Olou AA, Jack JL, Ruckert MT, Walsh RM, Eades AE, Bye BA, Ambrose J, Messaggio F, Anant S, VanSaun MN
Cell death & disease 2022 Feb 4;13(2):114

Identification of lamprey variable lymphocyte receptors that target the brain vasculature.

Lajoie JM, Katt ME, Waters EA, Herrin BR, Shusta EV
Scientific reports 2022 Apr 11;12(1):6044

Multiplexed non-invasive tumor imaging of glucose metabolism and receptor-ligand engagement using dark quencher FRET acceptor.

Rudkouskaya A, Sinsuebphon N, Ochoa M, Chen SJ, Mazurkiewicz JE, Intes X, Barroso M
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Free fatty acids receptors 2 and 3 control cell proliferation by regulating cellular glucose uptake.

Al Mahri S, Al Ghamdi A, Akiel M, Al Aujan M, Mohammad S, Aziz MA
World journal of gastrointestinal oncology 2020 May 15;12(5):514-525

AMPK-mediated senolytic and senostatic activity of quercetin surface functionalized Fe(3)O(4) nanoparticles during oxidant-induced senescence in human fibroblasts.

Lewinska A, Adamczyk-Grochala J, Bloniarz D, Olszowka J, Kulpa-Greszta M, Litwinienko G, Tomaszewska A, Wnuk M, Pazik R
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Molecular Imaging of Extracellular Tumor pH to Reveal Effects of Locoregional Therapy on Liver Cancer Microenvironment.

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Clinical cancer research : an official journal of the American Association for Cancer Research 2020 Jan 15;26(2):428-438

Interactions between TGF-β type I receptor and hypoxia-inducible factor-α mediates a synergistic crosstalk leading to poor prognosis for patients with clear cell renal cell carcinoma.

Mallikarjuna P, Raviprakash TS, Aripaka K, Ljungberg B, Landström M
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Acyl-CoA-Binding Protein Is a Lipogenic Factor that Triggers Food Intake and Obesity.

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Talreja J, Talwar H, Bauerfeld C, Grossman LI, Zhang K, Tranchida P, Samavati L
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Mfsd2a and Glut1 Brain Nutrient Transporters Expression Increase with 32-Week Low and High Lard Compared with Fish-Oil Dietary Treatment in C57Bl/6 Mice.

Sandoval KE, Wooten JS, Harris MP, Schaller ML, Umbaugh DS, Witt KA
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N-3PUFA differentially modulate palmitate-induced lipotoxicity through alterations of its metabolism in C2C12 muscle cells.

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Taïeb D, Barlier A, Yang C, Pertuit M, Tchoghandjian A, Rochette C, Zattara-Canoni H, Figarella-Branger D, Zhuang Z, Pacak K, Metellus P
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Verma R, Haldar C
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Catalani S, Carbonaro V, Palma F, Arshakyan M, Galati R, Nuvoli B, Battistelli S, Canestrari F, Benedetti S
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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis of GLUT1 on A. mouse kidney membrane protein and B. rat kidney membrane protein using Product # PA1-46152.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis of GLUT1 using a polyclonal antibody (Product # PA1-46152).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis of GLUT1 in mouse kidney membrane protein (lane A) and rat kidney membrane protein (lane B). Samples were incubated in GLUT1 polyclonal antibody (Product # PA1-46152).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot was performed using Anti-GLUT1 Polyclonal Antibody (Product # PA1-46152) and a ~55 kDa band corresponding to GLUT1 was observed across tissues tested . Membrane enriched extracts (30 µg lysate) of Mouse Kidney (Lane 1), Rat Kidney (Lane 2), Mouse Liver (Lane 3), Rat Liver (Lane 4) were electrophoresed using NuPAGE™ 4-12% Bis-Tris Protein Gel (Product # NP0322BOX). Resolved proteins were then transferred onto a Nitrocellulose membrane (Product # LC2002) by iBlot® 2 Dry Blotting System (Product # IB21001). The blot was probed with the primary antibody (2 µg/mL) and detected by chemiluminescence with Goat anti-Rabbit IgG (H+L) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A27036, 1:4000) using the iBright FL 1000 (Product # A32752). Chemiluminescent detection was performed using Novex® ECL Chemiluminescent Substrate Reagent Kit (Product # WP20005).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Immunohistochemical analysis of GLUT1 in formalin-fixed paraffin-embedded tissue section of human placenta. Samples were incubated in GLUT1 polyclonal antibody (Product # PA1-46152) using a dilution of 1:200. The staining was developed using HRP-DAB detection method and the sections were further counterstained with hematoxylin. This antibody generated a specific strong membrane cytoplasmic staining of Glut1 primarily in the syncytiotrophoblast layers of various villi and in the red blood cells (RBCs). Cytotrophoblasts showed a very weak expression of this protein.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Flow cytometry of GLUT1 in HepG2 and a matched isotype control. Samples were incubated in GLUT1 polyclonal antibody (Product # PA1-46152) using a dilution of 5 µg/mL for 30 minutes at room temperature followed by a Rabbit IgG (H+L) Cross-Adsorbed secondary antibody. Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: FIGURE 3 Western blot analysis bar charts show differences in Glut1 (~55 kDa) protein expression in cortical (A) and subcortical (D) brain tissue at the end of the 32-wk diet treatment. Representative blots of cortical (B) and subcortical (E) brain tissue with actin reprobes are shown. Deglycosylation evaluation blots of cortical (C) and subcortical (F) brain tissue show nondeglycosylated control (1) and deglycosylated (2) samples (41% lard). Values are means +- SEMs, n = 11-12/group. Two-factor ANOVA with Tukey-Kramer post hoc test was conducted when interactions were significant. *Different from 10% lard, P < 0.05. Glut-1, glucose-1 transporter Slc2a1.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 6 Western Blotting analysis of GLUT-1 receptor in Jurkat, U937, and K562 leukemia cell lines after 72 h of incubation with CF (5 mul/ml) as compared to untreated cells (control). Results are representative of three independent experiments.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 8 Immunohistochemical staining of consecutive tumor sections from M1 (A-D) , M2 (E-H) and M3 (I-L) tumor xenografts using hematoxylin and eosin (A, E & I) , anti-human transferrin (Tf) (B, F & J) , anti-human transferrin receptor (TfR) (C, G & K) and anti-glucose transporter 1 (GLUT1) (D, H & I) . NovaRED was used as peroxidase substrate (brown color), sections were counterstained with methyl green. White dashed lines delineate necrotic core (NC). Scale bar = 100 um.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Brain microvessel plasma membrane (BMPM) isolation and lamprey immunization validation. ( A ) Isolated mouse brain microvessels were stained with trypan blue. Scale bar = 25 mum. ( B ) Cropped western blots for Glut-1 and GFAP along with normalized GGT activity for the various fractions generated during BMPM isolation. Raw western blot data can be found in Fig. S11 . Hypotonic lysis was used to disrupt the isolated brain microvessels. Following centrifugation, the supernatant (HLS) was separated from the lysed microvessel fragments. Sonication of the microvessel fragments and centrifugation separated the plasma membranes (PM) from the basement membrane pellet (BM). ( C ) Pooled plasma from BBB immunized lampreys or a plasma sample from a naive lamprey were used to immunolabel mouse brain sections (red) and brains were counterstained with fluorescent IB 4 -lectin (green) to identify brain microvessels. Scale bar = 50 mum. ( D ) Glycan microarray analysis. Plasma samples from a naive lamprey (Naive, gray), lamprey immunized with human erythrocytes (RBC, blue), or BMPM immunized lamprey (BBB, red) were used to probe the CFGv5.2 glycan microarray. RFU = relative fluorescence units.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig. 6 MNPQ-mediated changes in the levels of HP-induced senescent cells (A) and the levels of selected proteins involved in cell signaling, proinflammatory responses, autophagy and glucose uptake (B, C). (A) Senescence-associated beta-galactosidase activity. Representative microphotographs are shown. Scale bars 100 mum, objective 20x. (B, C) Western blot analysis of the levels of AMPK, phospho-AMPK, LC3BII, IFN-beta, IL-8, AKT, phospho-AKT and GLUT1. For evaluation of LC3BII levels, cells were also incubated with 50 mug/ml chloroquine for 6 h. Data were normalized to beta-actin. Chloroquine-treated samples are denoted with an asterisk. The levels of phospho-AMPK and phospho-AKT are also presented as a ratio of phospho-AMPK to AMPK and phospho-AKT to AKT, respectively. IL-8 and IFN-beta levels in supernatants were calculated per 10000 cells. Bars indicate SD, n = 3, *** p < 0.001, ** p < 0.01, * p < 0.05 compared to CTRL, ### p < 0.001, ## p < 0.01, # p < 0.05 compared to HP-treated control (ANOVA and Dunnett's a posteriori test). CTRL , control conditions; Q , quercetin; MNP , magnetite nanoparticles; MNPQ , quercetin surface functionalized magnetite nanoparticles. Fig. 6

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 3. (a) Immunoblots show protein expression of HIF-1alpha, HIF-2alpha, GLUT-1, CA9, ALK5-full length (ALK5-FL), pSMAD2/3, SMAD2/3, and VHL after treatment with CoCl 2 (300 uM) at indicated time points in ACHN cells (n = 3 independent experiments). All protein bands in each lane originated from the same cell lysate. beta-actin served as an internal loading control. (b) Immunoblots show protein expression of HIF-1alpha, HIF-2alpha, GLUT-1, CA9, ALK5-full length (ALK5-FL), pSMAD2/3, and SMAD2/3, and VHL after treatment with CoCl 2 (300 uM) at indicated time points in A498 cells (n = 3 independent experiments). All protein bands in each lane originated from the same cell lysate. beta-actin served as an internal loading control.

PA1-46152

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