Recombinant Rat Endothelial PAS domain-containing protein 1 (Epas1), partial

Code CSB-YP864314RA
MSDS
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Source Yeast
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Code CSB-EP864314RA
MSDS
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Source E.coli
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Code CSB-EP864314RA-B
MSDS
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Source E.coli
Conjugate 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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Code CSB-BP864314RA
MSDS
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Source Baculovirus
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Code CSB-MP864314RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Epas1
Uniprot No.
Alternative Names
Epas1; Hif2aEndothelial PAS domain-containing protein 1; EPAS-1; Hypoxia-inducible factor 2-alpha; HIF-2-alpha; HIF2-alpha
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
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.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
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.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
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.
Gene References into Functions
  1. 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
  2. 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
  3. 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
  4. 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
  5. Demonstrate that iron deficiency augments megakaryocytic differentiation and proplatelet formation and suggest a potential role of HIF2alpha in megakaryopoiesis. PMID: 25715026
  6. 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
  7. HIF-2a accumulates earlier than Hif1a in bladder outlet obstruction PMID: 24589856
  8. 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
  9. 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
  10. 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
  11. Oxidative stress triggers increased HIF-1alpha protein levels in HIF-2alpha-deficient PC12 cells. PMID: 23610397
  12. 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
  13. 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
  14. In nucleus pulposus cells, HIF-1alpha and HIF-2alpha, degradation was mediated through 26S proteasome irrespective of oxygen tension. PMID: 21987385
  15. Glucose-induced O consumption creates an intracellular hypoxia that activates HIF1 and HIF2 in rat beta-cells PMID: 22235342
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. The differential expression of HIF1a, HIF2a, and HIF3a may play a role in the development of hypoxia-induced pulmonary hypertension. PMID: 16677454
  22. 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
  23. 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
  24. identified many novel HIF regulated genes with diverse functions in hypoxia mediated signaling and survival pathways PMID: 14747751
  25. 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
  26. 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
  27. 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
  28. expression in the carotid body during chronic hypoxia PMID: 16683694
  29. 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
  30. 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
  31. 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
  32. Activation of HIF-1alpha and HIF-2alpha contributes significantly to stretch- but not to shear-stress-induced capillary growth. PMID: 17627993
  33. In O2-sensitive adrenomedullary chromaffin cells mitochondrial O2 consumption regulates HIF-2alpha during hypoxia. PMID: 18353899
  34. 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
  35. Activation of hypoxia-inducible factors (HIF-1a and HIF-2a) ameliorates hypoxic distal tubular injury in the isolated perfused rat kidney. PMID: 18515655
  36. HIF-2 and HIF-1 modulate their own transcriptional activity through cited2 in nucleus pulposis PMID: 19035510
  37. 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
  38. Report increased prolyl 4-hydroxylase expression and differential regulation of hypoxia-inducible factors in the aged rat brain. PMID: 19420289
  39. 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
  40. 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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Subcellular Location
Nucleus. Nucleus speckle.
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