Recombinant Mouse Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1)

Name: Recombinant Mouse Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1)
Brand: Beta LifeScience
SKU: BLC-07807P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Solute Carrier Family 2, Facilitated Glucose Transporter Member 1 (SLC2A1) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17809
Target Symbol	SLC2A1
Synonyms	Glucose transporter type 1, erythrocyte/brain
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	KVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV
Expression Range	451-492aa
Protein Length	Partial
Mol. Weight	4.5 kDa
Research Area	Signal Transduction
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	KEGG: mmu:20525 STRING: 10090.ENSMUSP00000030398 UniGene: PMID: 30446646 Adequate Glut1 protein is indispensable for the proper development and maintenance of the capillary network of the brain. PMID: 28106060 GLUT1 may play an important role in Prostate Cancer progression via mediating glycolysis and proliferation. There is potential crosstalk between GLUT1-mediated glycolysis and androgen sensitivity in Prostate Cancer. PMID: 29105798 ARAP2 knockdown did not affect fatty acid uptake but reduced basal glucose uptake, total levels of the glucose transporter GLUT1, and GLUT1 levels in the plasma membrane and the lipid micro-domain fraction. PMID: 27476102 TBC1D5 shuttling to autophagosomes during metabolic stress facilitates retromer-dependent GLUT1 trafficking. PMID: 28602638 inhibition of GLUT1 activity and/or expression is shown to impair TGF-beta-driven fibrogenic processes, including cell proliferation and production of profibrotic mediators PMID: 27480571 B cell leukemia-induced inhibition of T cell Akt/mTORC1 signaling and glucose metabolism drives T cell dysfunction; metabolic defects included reduced Akt/mammalian target of rapamycin complex 1 (mTORC1) signaling, decreased expression of the glucose transporter Glut1 and hexokinase 2, and reduced glucose uptake PMID: 27511728 This study demonstrates a strict requirement for GLUT1 in the early stages of mammary tumorigenesis in vitro and in vivo. PMID: 27998284 GLUT1-dependent glycolysis regulates fibrogenesis in aged lung. PMID: 27997810 Data (including data from studies using transgenic mice) suggest that Glut1 (glucose transporter type 1) is a critical downstream target of Hif1a (hypoxia-inducible factor 1, alpha subunit) mediating hyperglycemia-induced extracellular matrix accumulation in kidney via regulation of Nox4 (NADPH oxidase type 4) expression in nephropathy due to diabetes type 1. PMID: 26908870 CRISPR/Cas9-mediated disruption of the Hdac2 gene increased Slc2a1 expression, suggesting that it is one of the responsible histone deacetylases (HDACs). These results confirm that b-OHB is a HDAC inhibitor and show that b-OHB plays an important role in fasting-induced epigenetic activation of a glucose transporter gene in the brain. PMID: 27935189 Taken together, the data suggest that curcumin binds directly to GLUT1 at a site that overlaps with the cytochalasin B binding site and thereby inhibits glucose transport. PMID: 27039889 overnutrition during early life induces short-term metabolic disturbances, impairment in heart insulin signaling, up-regulates GLUT-1 and switch cardiac fuel preference in juvenile mice PMID: 26608021 alpha(1)-AR activation is anti-apoptotic and protective during cardiac ischemia due to glucose deprivation and not hypoxia by enhancing glucose uptake into the heart via PKCdelta-mediated GLUT translocation that may be specific to the alpha(1A)-AR subtype. PMID: 26832303 Glut1 connects the enhanced glucose uptake in atheromatous plaques of ApoE(-/-) mice with their myelopoiesis through regulation of hematopoietic stem and multipotential progenitor cell maintenance and myelomonocytic fate. PMID: 26926469 Enhanced GLUT1 expression in melanoma cells favors their metastatic behavior. PMID: 26293674 bright-field microscopy designed to automatically identify and segment microvessels containing the protein glucose transporter 1. PMID: 26828723 Morphological changes and GLUT1, GLUT3, and GLUT4 expression were evaluated in placentas by immunohistochemical and image analysis and correlated with iAs and arsenical species concentration, which were quantified by atomic absorption spectroscopy PMID: 26339590 Nicotine pre-exposure reduced the ischemic-reperfusion-enhanced glucose transporter-1 function and expression at the blood brain barrier in a focal brain ischemia mouse model. PMID: 25925411 A lack of effect on gene expression, changes in the protein expression patterns of the key genes GLUT1/SLC2A1 and HK2 were observed after radiation treatment. PMID: 25304950 Glut1 deficiency decreased Teff expansion and the ability to induce inflammatory disease in vivo. PMID: 24930970 GLUT1 deficiency in cardiomyocytes does not accelerate the transition from compensated hypertrophy to heart failure. PMID: 24583251 Beta 3-adrenoceptors stimulate glucose uptake in brown adipose tissue via cAMP-mediated increases in GLUT1 transcription and synthesis and mTOR complex 2-stimulated translocation of newly synthesized GLUT1 to the plasma membrane. PMID: 25385184 GLUT1 brain levels in scrapie-infected animals was unchanged compared to controls. PMID: 24243341 Cysteine biochemistry is utilized in both methylene blue and berberine activation of glucose uptake by GLUT1. PMID: 24333987 glucose transporter 1 (GLUT1)-mediated glucose metabolism has a role in the proinflammatory phenotype PMID: 24492615 Placental endoplasmic reticulum stress by administration of Tun causes downregulation of Slc2a1(GLUT1) and upregulation of Slc2a3(GLUT3) mRNA expression. PMID: 24370435 Data indicate that tumor tissues from idh2-/- ((knock-out) mice had significantly decreased HIF-1alpha expression, blunted mRNA expression of HIF-1alpha, VEGF, and the glucose transport protein Glut-1 was also observed. PMID: 24240089 Quantitative real-time polymerase chain reaction revealed up-regulation of hypoxia and oxidative stress related genes, including Slc2a1. PMID: 23429070 Access to a running wheel for 48h induced plastic changes in the expression of astrocyte GLUT1. A significant increase was found only in motor cortex, though other motor related areas showed a similar trend(sensorimotor cortex, striatum and cerebellum). PMID: 23201358 Loss of neuronatin caused a reduction in both basal and insulin-stimulated glucose uptake and glycogen synthesis, likely mediated by a reduction in Glut1 protein upon silencing of neuronatin. PMID: 23482445 The results of this study demonstrated that valproic acid, a known histone deacetylases inhibitor, increased the glucose transport capacity in SLC2A1 heterozygous cerebral astrocytes of mice. PMID: 22532550 metabolite receptors (Slc2a1 and Ldr) were down-regulated in diet-induced obese mice PMID: 23001779 Heptanoate as a neural fuel: energetic and neurotransmitter precursors in normal and glucose transporter I-deficient (G1D) brain PMID: 23072752 GLUT1 siRNA blocked the 6-phenyl cAMP-induced increase in embryonic stem cell proliferation. PMID: 22658979 Report GLUT1 expression in normal left ventricle and in models of dilated and hypertophic cardiomyopathy. PMID: 22681646 Acute fasting decreases GLUT1 expression and glucose utilisation, inhibiting the processes of oocyte maturation and cumulus cell expansion. PMID: 22697123 Data show that an intense glucose transporter 1 (GLUT1)-immunoreaction was localized in the enamel organ of bud-stage molar tooth germs, where the active cell proliferation occurred. PMID: 22226978 Data suggest that GnRH up-regulates expression/localization of Glut1 (but not Glut2, Glut4, or Glut8) and stimulates glucose utilization in gonadotrophs; effects of GnRH on Glut1 mRNA expression are partly mediated by ERK activation/phosphorylation. PMID: 22107955 Studies demonstrate that GLUT1 is the major glucose transporter in mouse mammary carcinoma models overexpressing ErbB2 or PyVMT. PMID: 21826239 GLUT1 enhances mTOR activity independently of TSC2 and AMPK. PMID: 21613414 Fibroblast growth factor 21 induces glucose transporter-1 expression through activation of the serum response factor/Ets-like protein-1 in adipocytes PMID: 21846717 Data suggest that a portion of the hypoglycemic effects of berberine can be attributed to its acute activation of the transport activity of GLUT1. PMID: 21545824 The expression of GLUT1 in the ovary was generally weak with an intense expression of GLUT1 only in some vascular endothelia. PMID: 21360229 Findings suggest that GLUT1 mRNA expression is essential for decidualization. PMID: 21343253 Data show that CA9, GLUT1 and LOX mRNA levels were equally and strongly correlated to hypoxic extent in FaDudd, and the same was observed for CA9 and GLUT1, but not LOX, in SCCVII tumors. PMID: 21306648 adipose-specific deletion of SCD1 induces GLUT1 up-regulation in adipose tissue, suggesting that GLUT1 may play a critical role in controlling glucose homeostasis of adipose tissue in adipose-specific SCD1-deficient conditions. PMID: 20655875 GLUT1-VEGF-GLUT1 positive feedback loop may play a key role in contributing to renal disease in this model of nondiabetic glomerulosclerosis. PMID: 19918242 Expression is increased by exposure to tolbutamide in embryonic heart in vitro. Effect is concentration-dependent. PMID: 11835228 induction resulting from activation of prolyl hydroxylase oxygen-sensor PMID: 12649278

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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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