Product: GLUT1 Antibody
Catalog: AF5462
Description: Rabbit polyclonal antibody to GLUT1
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 45-60kDa; 54kD(Calculated).
Uniprot: P11166
RRID: AB_2837946

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(83%)
Clonality:
Polyclonal
Specificity:
GLUT1 Antibody detects endogenous levels of total GLUT1.
RRID:
AB_2837946
Cite Format: Affinity Biosciences Cat# AF5462, RRID:AB_2837946.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Choreoathetosis/spasticity episodic (paroxysmal choreoathetosis/spasticity); CSE; DYT17; DYT18; DYT9; EIG12; erythrocyte/brain; Erythrocyte/hepatoma glucose transporter; facilitated glucose transporter member 1; Glucose transporter 1; Glucose transporter type 1; Glucose transporter type 1, erythrocyte/brain; GLUT; GLUT-1; GLUT1; GLUT1DS; GLUTB; GT1; GTG1; Gtg3; GTR1_HUMAN; HepG2 glucose transporter; HTLVR; Human T cell leukemia virus (I and II) receptor; MGC141895; MGC141896; PED; RATGTG1; Receptor for HTLV 1 and HTLV 2; SLC2A1; Solute carrier family 2 (facilitated glucose transporter), member 1; Solute carrier family 2; Solute carrier family 2, facilitated glucose transporter member 1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P11166 GTR1_HUMAN:

Detected in erythrocytes (at protein level). Expressed at variable levels in many human tissues.

Description:
Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses.
Sequence:
MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Rabbit
100
Chicken
83
Xenopus
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P11166 As Substrate

Site PTM Type Enzyme
M1 Acetylation
N45 N-Glycosylation
S118 Phosphorylation
S226 Phosphorylation
T234 Phosphorylation
T238 Phosphorylation
K245 Ubiquitination
T258 Phosphorylation
S465 O-Glycosylation
S465 Phosphorylation
S473 Phosphorylation
K477 Sumoylation
K477 Ubiquitination
T478 Phosphorylation
S490 Phosphorylation

Research Backgrounds

Function:

Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain.

PTMs:

Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization.

Subcellular Location:

Cell membrane>Multi-pass membrane protein. Melanosome.
Note: Localizes primarily at the cell surface (PubMed:18245775, PubMed:19449892, PubMed:23219802, PubMed:25982116, PubMed:24847886). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Detected in erythrocytes (at protein level). Expressed at variable levels in many human tissues.

Subunit Structure:

Interacts with GIPC (via PDZ domain) (By similarity). Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via C-terminus cytoplasmic region) with DMTN isoform 2. Interacts with SNX27; the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with STOM. Interacts with SGTA (via Gln-rich region) (By similarity).

Family&Domains:

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily.

Research Fields

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Renal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.   (View pathway)

· Organismal Systems > Endocrine system > Insulin secretion.   (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

· Organismal Systems > Endocrine system > Glucagon signaling pathway.

References

1). Chitosan biguanide induced mitochondrial inhibition to amplify the efficacy of oxygen-sensitive tumor therapies. Carbohydrate Polymers (PubMed: 35989018) [IF=11.2]

2). Bruceine A induces cell growth inhibition and apoptosis through PFKFB4/GSK3β signaling in pancreatic cancer. PHARMACOLOGICAL RESEARCH (PubMed: 33992797) [IF=9.3]

Application: WB    Species: human    Sample: MIA PaCa-2 cells

Fig. 4. | Bruceine A induces cell growth inhibition and apoptosis via PFKFB4-mediated glycolysis in MIA PaCa-2 cells. (C) MIA PaCa-2 cells were treated with various concentrations of bruceine A for 24 h. Protein levels of GLUT1, HK2, PFKFB4, PFKM, PKM2, LDHA, and β-actin were detected. β-actin was served was as control. Results were expressed as means ± SD of three independent experiments. *p < 0.05, **p < 0.01, ***p < 0.001 versus control cultured with 0.1% DMSO by one-way ANOVA and post hoc tests.

3). Cisplatin conjugation with an exopolysaccharide extracted from Lactobacillus gasseri potentiates its efficacy and attenuates its toxicity. International Journal of Biological Macromolecules (PubMed: 36354077) [IF=8.2]

4). Pimozide inhibits the growth of breast cancer cells by alleviating the Warburg effect through the P53 signaling pathway. BIOMEDICINE & PHARMACOTHERAPY (PubMed: 35658233) [IF=7.5]

Application: WB    Species: Human    Sample: MCF-7 cells

Fig. 3. Pimozide inhibits PKM2 protein and mRNA in both MCF-7 and MDA-MB-231 cells in vitro. (A-B) Cells were treated with the indicated concentrations of Pimozide for 24 h, and the protein expression of glycolytic enzymes in MCF-7(A) and MDA-MB-231(B) cells were determined by Western blot analysis (left panel). Densitometry analysis was performed to assess the glycolytic enzymes protein expression (normalized to β-actin expression), PKM2 decreased significantly compared with untreated cells (right panel). (C-D) The mRNA expression of PKM2 in MCF-7(C) and MDA-MB-231(D) cells untreated or treated with Pimozide was determined by qRT-PCR. GAPDH was used as a control. Data represent mean ± SD from three biological replicates (*p < 0.05, **p < 0.01).

5). Inhibition of microRNA-327 ameliorates ischemia/reperfusion injury-induced cardiomyocytes apoptosis through targeting apoptosis repressor with caspase recruitment domain. JOURNAL OF CELLULAR PHYSIOLOGY (PubMed: 31587299) [IF=5.6]

6). Silencing of ANGPTL8 Alleviates Insulin Resistance in Trophoblast Cells. Frontiers in Endocrinology (PubMed: 34163433) [IF=5.2]

7). circATP2B1 Promotes Aerobic Glycolysis in Gastric Cancer Cells Through Regulation of the miR-326 Gene Cluster. Frontiers in Oncology (PubMed: 33996547) [IF=4.7]

8). Thioredoxin interacting protein (TXNIP) acts as a tumor suppressor in human prostate cancer. Cell Biology International (PubMed: 32639616) [IF=3.9]

Application: WB    Species: Human    Sample: prostate cancer tissues

Figure 7. TXNIP expression correlated inversely with GLUT1 expression in prostate cancer and TXNIP overexpression attenuated glucose uptake in the PC-3 cells. (A) GLUT1 protein expression level in 50 prostate cancer tissues were detected by IHC. (B) Negative correlation between TXNIP and GLUT1 mRNA expression patterns in prostate cancer tissues from TCGA cBioportal database. (C) The mRNA expression level of GLUT1 in normal prostatic epithelial cell line and prostate cancer cell lines was examined by qRT-PCR assay. (D and E) The protein expression level of GLUT1 in normal prostatic epithelial cell line and prostate cancer cell lines was examined by Western blot assay. (F) After overexpression of TXNIP in PC-3 cells, the mRNA expression level of GLUT1 was examined by qRT-PCR assay. (G and H) After overexpression of TXNIP in PC-3 cells, the protein expression level of GLUT1 was examined by Western blot assay. (I) The 2-NBDG glucose uptake demonstrated that TXNIP overexpression suppressed glucose uptake in PC-3 cells. The β-actin gene and protein were used as internal controls. Data represented the mean ± standard deviation of 3 independent experiments (*P < 0.05, **P < 0.01, ***P < 0.001).

9). Simulated microgravity led to increased brown adipose tissue activity in rats. Acta Astronautica [IF=3.5]

10). Bmi-1 directly upregulates glucose transporter 1 in human gastric adenocarcinoma. Open Life Sciences (PubMed: 35415241) [IF=2.2]

Application: IHC    Species: Human    Sample: GAC tissues

Figure 1 Bmi-1 and GLUT1 protein expression levels in (GAC) tissues and normal gastric specimens. Immunohistochemistry and western blot analysis were performed to examine the Bmi-1 and GLUT1 protein expression levels in GAC specimens (n = 4) and matched histologically normal gastric specimens (n = 4). Representative images of immunohistochemical staining of Bmi-1 in (a) GAC and (b) noncancerous control tissues (magnification, 400×). The yellow-brown color denotes positive Bmi-1 expression that is mainly located in the nucleus (arrows). Representative images of immunohistochemical staining of GLUT1 in (c) GAC and (d) noncancerous control tissues (magnification, 400×). GLUT1 is mainly localized in the cell membrane (arrows); (e) Western blot analysis of Bmi-1 and GLUT1 protein expressions in four paired tissues of GAC and noncancerous control tissues. The relative Bmi-1 and GLUT1 protein levels were normalized to GAPDH; (f) quantification of the Bmi-1 and GLUT1 protein expression levels in three independent experiments on the basis of the immunohistochemical and western blot images. The levels of Bmi-1 and GLUT1 were significantly greater in AGC tissues vs matched adjacent noncancerous tissues (3.903 ± 0.9363 vs 1.613 ± 0.760 and 2.480 ± 1.276 vs 1.945 ± 0.230, respectively) (All P < 0.05). T, tumor tissues; P, paracancerous, noncancerous tissues.

Application: WB    Species: Human    Sample: GAC tissues

Figure 1 Bmi-1 and GLUT1 protein expression levels in (GAC) tissues and normal gastric specimens. Immunohistochemistry and western blot analysis were performed to examine the Bmi-1 and GLUT1 protein expression levels in GAC specimens (n = 4) and matched histologically normal gastric specimens (n = 4). Representative images of immunohistochemical staining of Bmi-1 in (a) GAC and (b) noncancerous control tissues (magnification, 400×). The yellow-brown color denotes positive Bmi-1 expression that is mainly located in the nucleus (arrows). Representative images of immunohistochemical staining of GLUT1 in (c) GAC and (d) noncancerous control tissues (magnification, 400×). GLUT1 is mainly localized in the cell membrane (arrows); (e) Western blot analysis of Bmi-1 and GLUT1 protein expressions in four paired tissues of GAC and noncancerous control tissues. The relative Bmi-1 and GLUT1 protein levels were normalized to GAPDH; (f) quantification of the Bmi-1 and GLUT1 protein expression levels in three independent experiments on the basis of the immunohistochemical and western blot images. The levels of Bmi-1 and GLUT1 were significantly greater in AGC tissues vs matched adjacent noncancerous tissues (3.903 ± 0.9363 vs 1.613 ± 0.760 and 2.480 ± 1.276 vs 1.945 ± 0.230, respectively) (All P < 0.05). T, tumor tissues; P, paracancerous, noncancerous tissues.

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