Recombinant Glut1 Monoclonal Antibody (AN301125L)
For research use only.
| Verified Samples | Verified Samples in WB: HepG2 |
| Dilution | WB 1:10000-1:50000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Glut1 protein |
| Abbre | Glut1 |
| Synonyms | EIG, SLC2A, DYT, SLC2A1, CSE, DYT17, DYT18, DYT9, EIG12, GLUT, GLUT-1, GLUT1, GLUT1DS, HTLVR, PED, SDCHCN, Choreoathetosis/spasticity episodic (paroxysmal choreoathetosis/spasticity), erythrocyte/brain, Erythrocyte/hepatoma glucose transporter, facilitated glucose transporter member 1, Glucose transporter 1, Glucose transporter type 1, GLUTB, GT1, GTG1, Gtg3, GTR1, HepG2 glucose transporter, Human T cell leukemia virus (I and II) receptor, member 1, MGC141895, MGC141896, RATGTG1, Receptor for HTLV 1 and HTLV 2, Solute carrier family 2, Solute carrier family 2 (facilitated glucose transporter), CSE, DYT17, DYT18, DYT9, EIG12, GLUT, GLUT-1, GLUT1, GLUT1DS, HTLVR, PED, SLC2A1, GLUT-1 |
| Swissprot | |
| Calculated MW | 54 kDa |
| Observed MW |
50-300 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cell membrane, Multi-pass membrane protein, Melanosome, Photoreceptor inner segment, 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). |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cardiovascular, Cancer, Metabolism |
| Clone No. | 12G8 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene encodes a major glucose transporter in the mammalian blood-brain barrier. The encoded protein is found primarily in the cell membrane and on the cell surface, where it can also function as a receptor for human T-cell leukemia virus (HTLV) I and II. Mutations in this gene have been found in a family with paroxysmal exertion-induced dyskinesia. |
Other Clones
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Unconjugated
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