glut3 molecular weight

[1] GLUT3 facilitates the transport of glucose across the plasma membranes of mammalian cells. GLUT3 Glucose transporter 3 (or GLUT3 ), also known as solute carrier family 2, facilitated glucose transporter member 3 (SLC2A3) is a protein that in humans is encoded by the SLC2A3 gene. To date, no glucose transport activity has been reported for GLUT13, although it does appear to mediate inositol-3-phosphate (IP3) movement. Anti-Glucose Transporter Glut3 Antibody (G-5) is a mouse monoclonal IgG 1 Glucose Transporter Glut3 antibody, cited in 35 publications, provided at 200 g/ml raised against amino acids 216-265 mapping within an internal region of Glut3 of human origin The latter is also . Packaging, Storage & Formulations. Predicted molecular weight. Immunocytochemical studies demonstrated that binding sites for these antisera were abundantly distributed in neuropil in all brain regions. Following the same principle for the engineering of XylE-WW, we introduced two Trp substitutions, S64W and I305W, on the extracellular segments of TM2 and TM8 of GLUT3, respectively. Detects a band of approximately 54 kDa (predicted molecular weight: 54 kDa). Localization of glucose transporter GLUT 3 in brain: Comparison of rodent and dog using species-specific carboxyl-terminal antisera 70 The ubiquitous distribution of GLUT3 in human tissues suggests that it, together with GLUT1, may be responsible for basal glucose transport. Molecular Weight of Glut3: 48-70 kDa. Glucose Transporter GLUT3: Membrane. These findings reveal context-dependent druggable vulnerability in a subpopulation of GBM. Lin, C.C., et al. Entrez Gene . Alexa Fluor STORAGE Store at 4 C, **DO NOT FREEZE**. This antibody does not cross-react with Glut1, Glut2, or Glut4. Neuronal glucose transporter (GLUT) isoform 3 deficiency in null heterozygous mice led to abnormal spatial learning and working memory but normal acquisition and retrieval during contextual . 1/1000 - 1/10000. 80 kDa. Associated products. However this proposal, is implausible for two reasons. At the molecular level, we show that GLUT3-dependent glucose uptake controls a metabolic-transcriptional circuit that regulates the pathogenicity of Th17 cells. Glut3 (G-5)mouse, rat human Glut3 WB, IP, IF ELISA . its underlying molecular mechanisms in placental growth and function have rarely been investigated. Accordant with its high affinity for glucose, GLUT3 plays a pivotal role in the glucose uptake of cell types with a high demand for energy, such as sperm, circulating white blood cells, and preimplantation embryos (Simpson et al., 2007). Detects a band of approximately 54 kDa (predicted molecular weight: 54 kDa). Definite band of correct molecular weight Definite band of correct molecular weight for Glut3 observed by Western Blot using U-87 MG whole cell lysate. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. Glut3 (E7M7V) Rabbit mAb recognizes endogenous levels of total Glut3 protein. To further elucidate the role of GLUT3 in embryonic development, we utilized the vertebrate whole animal model system of Danio rerio as a tractable system for defining the cellular and molecular mechanisms altered by impaired glucose transport and metabolism related to perturbed expression of GLUT3. 44 GLUT13 is the only GLUT that has specific electrogenic transport activity for myo-inositol. We found that the glucose transporter GLUT3 is essential for the effector functions of Th17 cells in models of autoimmune colitis and encephalomyelitis. Validated in WB and tested in Mouse, Rat, Human. The rapamycin-sensitive mTOR complex 1 (mTORC1), but not the rapamycin-insensitive mTOR complex 2 . Species Reactivity: Human, Mouse, Rat Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu260 of human Glut1 protein. Furthermore, high GLUT3 expression remarkably increased the sensitivity of CRC cells to treatment with vitamin C and vitamin C-containing regimens. GTR14: Membrane. 2012. View Rabbit Polyclonal anti-Glut3 Antibody (NBP3-09984). What is the subcellular localization of GLUT3? . (MEFs) and human cancer cell lines consistently indicate that the expression of glucose transporter 3 (Glut3) is dramatically up-regulated by mTOR. Validated Applications: WB. We quantified the rapidity of disappearance of mRNA and protein from human skeletal muscle at room temperature and at 4C. The structure was determined by X-Ray diffraction and was measured at a resolution of 2.65 Angstroms [8]. GLUT3 is expressed in rat muscle, but this glucose transporter protein has not been identified previously in adult human skeletal muscle. however, interestingly, the mRNA expression levels for a glucose transporter (Glut3 . SELECT PRODUCT CITATIONS 1. In the ruminant placenta, glucose uptake and transfer are mediated by facilitative glucose transporters SLC2A1 (GLUT1) and SLC2A3 (GLUT3). Importantly, the population of 3/Glut3 high GSC models can be further separated into Glut3-addicted versus Glut3-nonaddicted subsets based on a gene signature and/or molecular subtype. Mechanistically, low-glucose stress dramatically upregulated GLUT3 via the AMPK/CREB1 pathway. Background Glucose transporters, including GLUT3, are multiple-pass integral membrane proteins. GTR14: Membrane. SDS-PAGE - Recombinant Human Glucose Transporter GLUT3 protein (ab152681) 12.5% SDS-PAGE analysis of ab152861 stained with Coomassie Blue. Non-hazardous. Anti-Glucose Transporter GLUT3 antibody . SLC2A1 is located on the basolateral trophoblast membrane, whereas SLC2A3 is located solely on the maternal-facing, apical trophoblast membrane. Substitution of GLUT3 TM9 with GLUT1 TM9 causes chimeric GLUT3 to resolve as 6- and 10-nm Stokes radius particles. GLUT3 protein migrating at an apparent molecular mass of 49 kDa was detected by immunoblotting in membranes from whole placenta and endothelial cells derived from intraplacental microvessels, but not in isolated trophoblast cells. Amino acids. : 2015-05-03. Species Reactivity: Human Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala472 of human Glut3 protein. Studies with GLUTs expressed in and solubilized from HEK cells show that HEK cell GLUT1 resolves as 6- and 10-nm Stokes radius particles, whereas GLUT3 resolves as a 6-nm particle. 1 to 496. 1 Department of Biochemistry & Molecular Biology, School of Basic Medicine, Anhui Medical . Using Western blotting GLUT3 was detected as an integral membrane protein at a molecular weight of 50 kDa in microvillous membranes from all trimesters but not in syncytial basal membranes. . Formaldehyde-fixed, paraffin-embedded human testis tissue stained for Glucose Transporter GLUT3 using ab15311 at 1/200 dilution in immunohistochemical analysis. Based . A form of left ventricular non-compaction, a cardiomyopathy due to myocardial morphogenesis arrest and characterized by a hypertrophic left ventricle, a severely thickened 2-layered myocardium, numerous prominent trabeculations, deep intertrabecular recesses, and poor systolic function. -SCBT QC. Clinical manifestations are variable. Glut1 (D3J3A) Rabbit mAb recognizes endogenous levels of total Glut1 protein. Validated Species: Human. Rabbit recombinant monoclonal Glucose Transporter GLUT3 + GLUT14 antibody [EPR10508(N)] - N-terminal. GLUT3 was detected in the syncytiotrophoblast at all gestational ages by immunohistochemistry. This antibody does not cross-react with Glut2, Glut3, or Glut4. Notably, GLUT3 had a greater impact on cell growth than GLUT1 under glucose-limiting stress. No MSDS required. With aging, Glut3 reactivity was significantly decreased in the inner molecular layer of the hip-pocampal dentate gyrus (-46%) and the mossy fibers of the CA3 sector (-34%), whereas the . Mw, molecular weight marker. Cellular localization. Validated Species: Human. C, Glut1 and Glut3 expression (mean SD) in different cell-sorted populations from healthy lung or spleen, or from the CD45 fraction of lung tumors. Validated Applications: WB. They found GLUTs 3 (a reactive band of 45 kDa) and 5 (2 bands, 35 and 45 kDa), as well as the sodium-glucose transporter SGLT-1 (2 bands of 50-60 kDa), in dog sperm membrane, in which the location of these transporters, as already seen in human, rat, and bull spermatozoa, is specific for each protein. First, the K m of blastocyst glucose transport [6.3 0.5 mM for 3-O-methyl glucose (3-OMG) ()] is much lower than that of GLUT1 [20.1 2.9 mM for 3-OMG ()], suggesting the presence of a more efficient isoform.Second, in other polarized epithelial cells, GLUT1 is targeted to basolateral, rather than apical membrane domains (11, 12). Furthermore, in the OE, a low molecular weight GLUT1 (45 kDa) was found, unlike the low and high (55 kDa) molecular weight GLUT1. GLUT3 has a high affinity for glucose ( Km ~ 1.5 mM) and has the highest calculated turnover number of the GLUT isoforms, thus ensuring efficient glucose uptake. GLUT3 ( 5c65) is a transport protein consisting of 481 amino acids and weighing 52,520 Daltons in its asymmetrical unit [7]. We aligned the native GLUTs with their QTY variants. F, Western blot analysis of GLUT1 from HLNs and TANs. Target. Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Glucose Transporter GLUT3 antibody (ab15311) This image is courtesy of an anonymous Abreview. The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. This is because Q, T, Y amino acids do . Positive Controls: Hep G2 cell lysate: sc-2227 or U-87 MG cell lysate: sc-2411. The glycosylated isoform (55 kDa) of GLUT1 is expressed in BBB endothelial cells, while the other, lower molecular weight one (45 kDa) is located in astrocyte end-feet [3]. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Immunoblots of brain membrane preparations showed that both antisera identified peptide-inhibitable protein bands of molecular weight 45,000-50,000. GLUT13 is expressed mainly in the brain, in particular in ganglion cells and some neurons. Related Products. The link between GBM molecular subtype and response to treatment remains undefined. Human GLUT3 was initially cloned by low-stringency hybridization from a fetal skeletal muscle cell line, using a GLUT1 cDNA probe, and was found to share 64.4, 51.6, and subsequently 57.5% identity with GLUT1, -2, and -4, respectively ( 62 ). GLUT3 can be N-glycosylated. There are no reviews for Glut3 Partial Recombinant Protein (H00006515-Q01). This variant. The results showed that dietary supplementation with MT increased placental weight, while the percentage of piglets born with weight < 900 g decreased. . . Cellular localization. Database links. Stable for one year from the date of shipment. Our results confirmed the OE expression of GLUT1 and 3. Only the 3/Glut3 high GSC models with proneural/classical subtype markers are sensitive to inhibitors that target elements of the v3/PAK4/YAP pathway. View Rabbit Polyclonal anti-Glut3 Antibody (NBP3-09953). D and E, Real-time PCR analyses of Glut1 and Glut3 expression (mean SD) in HLNs compared with TANs. Database . This protein is an alpha-helical protein consisting of two chains, two different ligands and water [7]. Here, we present a 2.4 crystal structure of GLUT1 in an inward . Despite significant QTY replacement of hydrophobic residues overall (~17-26%), especially in the transmembrane domains (~44-50%) in the GLUTs, the isoelectric-focusing point pI and molecular weight remain rather similar (Figs 1 and 2 and Table 3). While SLC2A3 is less abundant than SLC2A1, SLC2A3 has a five-fold greater affinity and transport capacity. In this issue of Cancer Cell, Cosset and colleagues define a subpopulation of patients within the proneural/classical subtype sensitive to integrin blockade because of a Glut3 addiction. The molecular weight of GLUT3 transporter is 49-52 kDa and depends on the glycosylation pattern, which is tissue-specific (PMID: 9253355 and 9889355). Anti-Glucose Transporter GLUT3 + GLUT14 antibody [EPR10508(N)] - N-terminal at 1/10000 dilution Lane 1 : SH-SHY5Y cell lysate Lane 2 . Glucose Transporter GLUT3: Membrane. Target.

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