|Reactivity||Human, Mouse, Rat|
|Product Name||Anti-Glucose Transporter GLUT1/SLC2A1 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Solute carrier family 2, facilitated glucose transporter member 1(SLC2A1) detection. Tested with WB in Human;Mouse;Rat.|
|Cite This Product||Anti-Glucose Transporter GLUT1/SLC2A1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1120-1)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human SLC2A1(477-492aa KTPEELFHPLGADSQV), identical to the related mouse and rat sequences.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-SLC2A1 antibody, PA1120-1, Western blotting
All lanes: Anti SLC2A1(PA1120-1) at 0.5ug/ml
Lane 1: Rat Liver Tissue Lysate at 50ug
Lane 2: SW620 Whole Cell Lysate at 40ug
Lane 3: 293T Whole Cell Lysate at 40ug
Predicted bind size: 57KD
Observed bind size: 57KD
Protein Target Info (Source: Uniprot.org)
|Protein Name||Solute carrier family 2, facilitated glucose transporter member 1|
|Tissue Specificity||Detected in erythrocytes (at protein level). Expressed at variable levels in many human tissues. .|
|Alternative Names||Solute carrier family 2, facilitated glucose transporter member 1;Glucose transporter type 1, erythrocyte/brain;GLUT-1;HepG2 glucose transporter;SLC2A1;GLUT1;|
|Subcellular Localization||Cell membrane; Multi-pass membrane protein. Melanosome. Localizes primarily at the cell surface. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.|
|Molecular Weight||54084 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||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. .|
|Research Areas||Channels, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathways, Metabolism, Pathways And Processes, Plasma Membrane, Signal Transduction
*You can search these to find other products in these research areas.
|Background||GLUT1, also known as SLC2A1, is a major glucose transporter in the mammalian blood-brain barrier whose gene is mapped to 1p35-p31.3 and contains 10 exons. It is present at high levels in primate erythrocytes and brain endothelial cells. Not only can transport dehydroascorbic acid(the oxidized form of vitamin C) into the brain1, GLUT1 is also likely to contribute to HTLV-associated disorders through interacting with HTLV envelope glycoproteins. Functionally, GLUT1 deficiency causes a decrease in embryonic glucose uptake and apoptosis, which may be involved in diabetic embryopathy, by contrast, an increased expression of GLUT1 in some malignant tumors may suggest a role for glucose-derivative tracers to detect in vivo thyroid cancer metastases by positron-emission tomography scanning.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,