Recombinant Rat Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01133P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Rat Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01133P
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Product Overview

Description Recombinant Rat Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P11167
Target Symbol SLC2A1
Synonyms (Glucose transporter type 1, erythrocyte/brain)(GLUT-1)
Species Rattus norvegicus (Rat)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence CPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQEMKEEGRQMMREKKVTILELFRSPAYRQP
Expression Range 207-271aa
Protein Length Partial
Mol. Weight 15.2 kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors.
Subcellular Location Cell membrane; Multi-pass membrane protein. Photoreceptor inner segment.
Protein Families Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily
Database References
Tissue Specificity Detected in osteoblastic cells (at protein level). Detected in brain, and at lower levels in kidney, heart and lung.

Gene Functions References

  1. Increased Rat Placental Fatty Acid, but Decreased Amino Acid and Glucose Transporters Potentially Modify Intrauterine Programming PMID: 26590355
  2. The data of this study provided evidence that histone deacetylation may contribute toward the loss of GLT-1 PMID: 26953753
  3. Increased GLUT1 expression was observed together with overproduction of NO and pronounced liver injury in severely hyperglycaemic rats. GLUT1 overexpression might be implicated in the toxic effects of glucose in the liver. PMID: 26347179
  4. The GLUT1 plays a role in regulation of ROS and could contribute to maintenance of insulin action in the presence of ROS. PMID: 25101238
  5. In the cerebral cortex, GLUT1 increased at 18 h postexercise. PMID: 24610532
  6. Ezrin is down-regulated in diabetic kidney glomeruli and regulates actin reorganization and glucose uptake via GLUT1 PMID: 24726496
  7. Ascorbic acid markedly upregulated the basal expression of GLUT1 in endothelial cells of nondiabetic and diabetic cortex, which did not affect total ascorbic acid levels in the cortex. PMID: 24739976
  8. Hypothalamic GLUT1 mRNA abundance increases with age and is sexually dimorphic PMID: 24382486
  9. The expression of glut1 and glut4 in brain areas was not down-regulated, however, we observed trend to phase advance in glut1 expression in the cerebellum. PMID: 24329691
  10. The aim of the work was to evaluate GLUT1 and GLUT2 in kidneys of an animal model of metabolic syndrome. PMID: 24062089
  11. GLUT1 content is reduced in kidney cortex in diabetic hypertensive rats after blockade of the renin-angiotensin system, a phenomenon not specifically related to decreased blood pressure levels. PMID: 23680377
  12. The Akt/TSC/mTOR/S6K signaling pathway may be one of the mechanisms underlying the upregulation of GLUT1 expression in uremic vascular smooth muscle cells. PMID: 23265586
  13. CoCl(2) can increase mRNA expressions of GLUT1 and GLUT3 and glucose transporter activity of neurons in hypoxic conditions. PMID: 12506324
  14. that n-3 deficiency repressed GLUT1 gene expression in the cerebral cortex PMID: 22579067
  15. Progesterone could increase the tolerance of neurons to hypoxic-ischemia by up-regulating GLUT1 and GLUT3 expression. PMID: 21141602
  16. We found that although cocaine withdrawal decreases GLT1 expression in both core and shell of the nucleus accumbens, only in core is GLT1 downregulation sensitive to both access and withdrawal PMID: 22433294
  17. Data suggest that triiodothyronine (T3) up-regulates Glut1 and Glut3 in osteoblasts; thus, increased glucose uptake induced by T3 may be mediated by these high-affinity glucose transporters. PMID: 22258767
  18. The expression of GLUT4 was lower in older animals, but no relation between age and GLUT1 expression was found. PMID: 22125125
  19. During status epilepticus GLUT1 expression is increased throughout the brain between 1 and 12 hours, occurring more strongly in adult rats. PMID: 21624469
  20. GLUT1 enhances mTOR activity independently of TSC2 and AMPK. PMID: 21613414
  21. GLUT1 expression was statistically unchanged on the ketogenic diet. PMID: 21605500
  22. Sustained hyperglycemia impairs hypothalamic glucose sensing to lower glucose production through changes in hypothalamic glial GLUT1. Data highlight the critical role of hypothalamic glial GLUT1 in mediating glucose sensing to regulate glucose production. PMID: 21562080
  23. Results indicate that CHAs(OH) and water use a common translocation pathway in GLUT1 that is different to that of glucose transport. PMID: 21069159
  24. Increased podocyte GLUT1 expression in diabetic mice does not contribute to early diabetic nephropathy. It protects against mesangial expansion and fibronectin accumulation possibly by blunting podocyte VEGF increases. PMID: 20375116
  25. The mRNA and protein expression of GLUT1 in brain tissue increased significantly after hypoxic-ischemia. PMID: 19950593
  26. GLUT1 and GLUT3 expression was notably up-regulated in the penumbra region after cerebral ischemia. PMID: 19781384
  27. gene expression regulation by Sp1 in differentiating trophoblasts PMID: 11689000
  28. Enhanced placental GLUT1 and GLUT3 expression in dexamethasone-induced fetal growth retardation PMID: 11738800
  29. abundant in the occludin-positive endothelial cells of the nasal olfactory mucosa PMID: 11751462
  30. Glucose deprivation and hypoxia increase the expression of the GLUT1 glucose transporter via a specific mRNA cis-acting regulatory element. PMID: 11906001
  31. Glut1 is localized in astrocytic processes around axonal or dendritic elements of glutamatergic axo-dendritic synaptic junctions in the frontoparietal somatosensory cortex. PMID: 11950769
  32. Lactate-induced translocation of GLUT1 and GLUT4 is not mediated by the phosphatidyl-inositol-3-kinase pathway in the rat heart. PMID: 12002265
  33. Glucose transport was associated with enhanced accessibility of GLUT1 to its substrate and with photolabelling of formerly 'cryptic' exofacial substrate binding sites in GLUT1 molecules. PMID: 12006627
  34. Gene expression in the jejunum in response to insulin-like growth factors in rat pups. PMID: 12388463
  35. GLUT1 protein localised to the cytoplasm and basolateral surface of mammary epithelial cells in lactating rats PMID: 12483288
  36. Insulin-induced translocation of facilitative glucose transporters in fetal/neonatal rat skeletal muscle PMID: 12531786
  37. Upregulation of GLUT-1 expression: Link between hemodynamic and metabolic factors in glomerular hypertension? PMID: 12771048
  38. upregulation of GLUT1 serves a role in agonist-induced hypertrophy and survival which can be dissociated from its role in glucose transport PMID: 14519432
  39. A close correlation was found between local MCT1 and local GLUT1 densities. As local GLUT1 densities reflect local glucose metabolism in the brain, we conclude that local MCT1 densities are adjusted to local glucose metabolism and transport. PMID: 14729246
  40. Glucose uptake by way of 2-deoxyglucose and GLUT-1 transporter protein content was measured in basal and insulin-stimulated skeletal muscle cells. PMID: 14741039
  41. TATA box in the promoter of the GLUT1 gene is required by the agonist to activate transcription from the promoter. PMID: 15808844
  42. GLUT1 and GLUT8 are both expressed in prepubertal testis, but only GLUT1 is regulated by l-triiodothyronine (T(3)); also found that the effect of T(3) cannot be attributed to its action on GLUT1 promoter PMID: 15811071
  43. The impact on urinary TGF-beta1 occurs when diabetes and hypertension are associated, suggesting an effect that is triggered in the presence of GLUT1 overexpression and hyperglycemia. PMID: 15855808
  44. Levels of both GLUT1 and GLUT12 are elevated in animal models of hypertension and diabetic nephropathy. PMID: 16091581
  45. Decreased glucose utilization in the cerebral cortex of (n-3) PUFA-deficient rats is due to reduced amounts of the 2 isoforms of GLUT1, indicating post-transcriptional regulation of GLUT1 synthesis. PMID: 16140905
  46. Data show that the consensus Sp1 site located in the rat proximal glucose transporter (Glut)1 promoter is necessary and sufficient for basal expression of the Glut1 gene, as well as for its response to hyperosmolarity. PMID: 16162661
  47. Findings suggest the presence of GLUT1 in detergent-resistant membrane domains of spermatogenic cells, and support a role for caveolae in relation to glucose uptake and glucose phosphorylation. PMID: 16419038
  48. susceptibility to diabetic glomerulopathy in MNS rats is associated with increased GLUT1-dependent glucose transport activity in response to hyperglycaemia and/or TGF-beta, which may amplify ECM overproduction. PMID: 16449286
  49. results indicate that AQP4 may play a much more important role in blood-brain barrier function than GLUT-1, and thereby also in water distribution in the cerebral cortex of stroke-prone spontaneously hypertensive rats with severe hypertension PMID: 16461188
  50. the regulation of GLUT1 and GLUT3 in cerebral cortex is regulated by T(3)and the expression of glucose transporters induced by hypothyroidism might have a functional impact on brain glucose uptake. PMID: 16581179

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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