Recombinant Rat Endothelial PAS domain-containing protein 1 (Epas1), partial
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中文名稱:大鼠Epas1重組蛋白
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貨號:CSB-YP864314RA
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規(guī)格:
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來源:Yeast
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其他:
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中文名稱:大鼠Epas1重組蛋白
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貨號:CSB-EP864314RA
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規(guī)格:
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來源:E.coli
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其他:
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中文名稱:大鼠Epas1重組蛋白
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貨號:CSB-EP864314RA-B
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規(guī)格:
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來源:E.coli
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共軛:Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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其他:
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中文名稱:大鼠Epas1重組蛋白
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貨號:CSB-BP864314RA
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規(guī)格:
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來源:Baculovirus
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其他:
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中文名稱:大鼠Epas1重組蛋白
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貨號:CSB-MP864314RA
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規(guī)格:
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來源:Mammalian cell
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其他:
產(chǎn)品詳情
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純度:>85% (SDS-PAGE)
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基因名:
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Uniprot No.:
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別名:Epas1; Hif2aEndothelial PAS domain-containing protein 1; EPAS-1; Hypoxia-inducible factor 2-alpha; HIF-2-alpha; HIF2-alpha
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種屬:Rattus norvegicus (Rat)
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蛋白長度:Partial
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蛋白標(biāo)簽:Tag?type?will?be?determined?during?the?manufacturing?process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially. -
產(chǎn)品提供形式:Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. -
復(fù)溶:We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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儲存條件:Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保質(zhì)期:The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. -
貨期:Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
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注意事項(xiàng):Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet :Please contact us to get it.
靶點(diǎn)詳情
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功能:Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD.
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基因功能參考文獻(xiàn):
- Over-expressed lenti-EPAS1 can promote angiogenesis via the up-regulation of EPAS1-related angiogenic factors in the muscles of the affected hind limb and reduce gait disturbance. PMID: 29268860
- HIF-1alpha to HIF-2alpha switch in glycolytic gastrocnemius muscle in chronic kidney disease might be a protective mechanism against tissue hypoxia and oxidative stress. PMID: 28820398
- ZnCl2 (10 mg/kg) significantly lowered the creatinine and urea concentrations compared to saline-treated control rats following a clinically relevant 60 minutes of ischemia. Zn2+ induced expression of HIF1a and HIF2a but not HIF3a.ZnCl2 preconditioning protects against renal Ischemia-reperfusion injury in a dose-dependent manner PMID: 28686686
- Thirty-five days of chronic intermittent hypoxia up-regulated HIF-1alpha in the liver and down-regulated HIF-1alpha and HIF-2alpha in skeletal muscle. We concluded that the effect of chronic intermittent hypoxia on insulin sensitivity and signaling is time-dependent and is associated with changes in HIF signaling in insulin-sensitive tissues. PMID: 26993367
- Demonstrate that iron deficiency augments megakaryocytic differentiation and proplatelet formation and suggest a potential role of HIF2alpha in megakaryopoiesis. PMID: 25715026
- Results showed that the inhibitory effects of TNFa on the hypoxia-induced upregulation of erythropoietin expression are mediated primarily by HIF-2a rather than HIF-1a PMID: 25283246
- HIF-2a accumulates earlier than Hif1a in bladder outlet obstruction PMID: 24589856
- This investigation has thus revealed a novel aspect of Atp7a gene regulation in which Sp1 may be necessary for the HIF-mediated induction of gene transcription during iron deficiency/hypoxia. PMID: 23814049
- inhibition of HIF-1/2alpha did not reverse the effects of hypoxia on IL-6 gene expression. In addition, phosphorylation of p38, but not JNK, was responsible for the effects of glucose deprivation on IL-6 gene expression. PMID: 23520526
- In chronically hypoxic PC12 cells glycolytic energy budget, increased energy preservation and low susceptibility to OGD are observed. HIF-2alpha no longer orchestrates adaptive responses to anoxia. PMID: 23462283
- Oxidative stress triggers increased HIF-1alpha protein levels in HIF-2alpha-deficient PC12 cells. PMID: 23610397
- Rgs4 transcript is readily detected but does not respond to hypoxia. Furthermore, this regulation was found to be dependent on transcription, and occurs in a manner consistent with direct HIF transactivation of Rgs4 transcription PMID: 22970249
- Uppregulation of both HIF-2alpha and Kir6.2 is confined to medullary, but not cortical, tissue in adrenal chromaffin cells following prenatal nicotine exposure. PMID: 22403787
- In nucleus pulposus cells, HIF-1alpha and HIF-2alpha, degradation was mediated through 26S proteasome irrespective of oxygen tension. PMID: 21987385
- Glucose-induced O consumption creates an intracellular hypoxia that activates HIF1 and HIF2 in rat beta-cells PMID: 22235342
- HIF-1alpha and HIF-2alpha signaling and oxygen tension at the surface of cells were important in regulating the phenotype of rat alveolar type II cells. PMID: 21454802
- These results suggest that the translation of HIF-2alpha in the liver is regulated in part by the action of iron regulatory proteins in response to dietary iron deficiency. PMID: 21753061
- in b/b rats depressed liver hepcidin production and activated intestinal Hif2alpha starting at the C-pole resulted in increasing expression of iron transport genes, including DMT1 G185R, in an attempt to compensate for the anemia in Belgrade rats. PMID: 21436314
- Data show that the Atp7a gene is upregulated by direct interaction with HIF2alpha, demonstrating coordinate regulation with genes related to intestinal iron homeostasis. PMID: 21346155
- Suggest that increased vein wall tension induces HIF overexpression and causes an increase in MMP expression and reduction of venous contraction, leading to progressive venous dilation and varicose vein formation. PMID: 21106323
- The differential expression of HIF1a, HIF2a, and HIF3a may play a role in the development of hypoxia-induced pulmonary hypertension. PMID: 16677454
- retinal HIF-1alpha and HIF-2alpha were not found to be increased, and the extent of hypoxia may even decrease after 12 weeks of hyperglycemia in rats. PMID: 20005221
- rat pheochromocytoma PC12 cells, nerve growth factor (NGF) stimulation results in a decrease of both basal and hypoxia-induced levels of HIF-2 alpha protein. NGF treatment did not increase HIF-hydroxylase gene expression or activity, and the reduction of PMID: 12805361
- identified many novel HIF regulated genes with diverse functions in hypoxia mediated signaling and survival pathways PMID: 14747751
- Marked nuclear accumulation of HIF-1alpha and -2alpha occurred after both systemic hypoxia and coronary ligation in cardiomyocytes as well as interstitial and endothelial cells (EC) without pronounced changes in HIF mRNA levels PMID: 15247145
- HIF-1alpha, HIF-2alpha and HIF-3alpha may not only confer different target genes, but also play key pathogenetic roles in hypoxic-induced pulmonary hypertension. PMID: 16215633
- Hypoxia stimulates translation of HIF-1alpha and -2alpha proteins by distributing their mRNAs to larger polysome fractions. This requires influx of extracellular calcium, stimulation of classical protein kinase C-alpha, & mTOR activity. PMID: 16507764
- expression in the carotid body during chronic hypoxia PMID: 16683694
- hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha stabilization and transactivation in a graded oxygen environment are regulated in a cell-specific manner PMID: 16760477
- HIF-alpha subunits and prolyl hydroxylases show differential and reciprocal regulation, which might play a key pathogenesis role in hypoxia-induced pulmonary hypertension PMID: 16761101
- HIF2alpha C-terminal transactivation domain, in contrast to the HIF1alpha C-terminal transactivation domain, is relatively resistant to the inhibitory effects of FIH1 under normoxic conditions PMID: 17220275
- Activation of HIF-1alpha and HIF-2alpha contributes significantly to stretch- but not to shear-stress-induced capillary growth. PMID: 17627993
- In O2-sensitive adrenomedullary chromaffin cells mitochondrial O2 consumption regulates HIF-2alpha during hypoxia. PMID: 18353899
- HIF-1alpha/-2alpha had distinct spatial expression patterns in rat model of ischemic heart disease. Both HIF subunits might be potent stimuli for cardiomyocytes to re-enter the cell cycle and initiate DNA synthesis. PMID: 18484163
- Activation of hypoxia-inducible factors (HIF-1a and HIF-2a) ameliorates hypoxic distal tubular injury in the isolated perfused rat kidney. PMID: 18515655
- HIF-2 and HIF-1 modulate their own transcriptional activity through cited2 in nucleus pulposis PMID: 19035510
- Intermittent hypoxia leads to down-regulation of HIF-2alpha via a calpain-dependent signaling pathway and results in oxidative stress as well as autonomic morbidities. PMID: 19147445
- Report increased prolyl 4-hydroxylase expression and differential regulation of hypoxia-inducible factors in the aged rat brain. PMID: 19420289
- A basal level of HIF-2alpha is required for normal developmental expression of DOPA decarboxylase and dopamine beta hydroxylase; loss of this function leads to impaired catecholamine biosynthesis. PMID: 19457096
- adaptation to hypoxia exerts a protective role on cardiomyocytes subjected to ischemia and that, unexpectedly, this form of preconditioning absolutely depends on Hif-2alpha. PMID: 19461047
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亞細(xì)胞定位:Nucleus. Nucleus speckle.
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