SAB4502803
Anti-GLUT1 antibody produced in rabbit
affinity isolated antibody
Synonym(s):
GLUT-1, Glucose transporter type 1 erythrocyte/brain, HepG2 glucose transporter, SLC2A1, Solute carrier family 2 facilitated glucose transporter member 1
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA, IHC, WB
Citations:
14
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 54 kDa
species reactivity
mouse, human, rat
concentration
~1 mg/mL
technique(s)
ELISA: 1:40000, immunohistochemistry: 1:50-1:100, western blot: 1:500-1:1000
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SLC2A1(6513)
General description
Anti-GLUT1 Antibody detects endogenous levels of total GLUT1 protein.
GLUT1 (Glucose transporter type 1) gene is located on human chromosome 1p34.2. It is expressed in cerebral endothelial cells.
Immunogen
The antiserum was produced against synthesized peptide derived from human GLUT1.
Immunogen Range: 441-490
Immunogen Range: 441-490
Application
Anti-GLUT1 antibody produced in rabbit has been used
- for protein extraction
- in western blotting
- for immunohistochemistry
Anti-GLUT1, C-Terminal antibody is suitable for use in western blot and immunohistochemistry.
Biochem/physiol Actions
GLUT1 (Glucose transporter type 1) functions as a receptor for human T-cell leukemia virus (HTLV) I and II. It plays a key role in HTLV-envelope mediated infection. GLUT1 is associated with paroxysmal exertion-induced dyskinesia. Glut1 may regulate cerebral microvasculature, proliferation of endothelial cells and the development of junctional complexes of the BBB (blood-brain barrier). It transports glucose across the BBB.
GLUT1 is a membrane protein that regulates the facilitative transport of glucose across the cells. Mutations in the gene encoding GLUT1 have been linked to epilepsy and diabetic nephropathy . Increased expression of GLUT1 has been associated with tumor differentiation in breast and endometrial cancers, whereas decreased GLUT1 function causes GLUT1 deficiency syndrome . Anti-GLUT1, C-Terminal antibody can be used to detect endogenous levels of total GLUT1 protein. The antibody specifically reacts with GLUT1 in mice, rats and humans.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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Yang Li et al.
Molecular metabolism, 66, 101630-101630 (2022-11-08)
Bone is a highly dynamic organ that undergoes constant bone formation and remodeling, and glucose as a major nutrient is necessary for bone formation and remodeling. Retinoblastoma (Rb1) is a critical regulator of mesenchymal stem cells (MSCs) fate, but how
Valeria Meier et al.
PloS one, 11(2), e0149993-e0149993 (2016-02-26)
For various types of tumor therapy, it is suggested that co-targeting of tumor microenvironment, mainly tumor vasculature, mediates tumor response mechanisms. Immunohistochemistry for glucose transporter-1 (GLUT-1), carbonic anhydrase-IX (CAIX), Ki-67, and von Willebrand factor VIII for microvessel density (MVD) were
Glucose modulation induces reactive oxygen species and increases P-glycoprotein-mediated multidrug resistance to chemotherapeutics
Seebacher NA, et al.
British Journal of Pharmacology, 172(10), 2557-2572 (2015)