Recombinant Mouse Endothelial PAS domain-containing protein 1 (Epas1), partial
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中文名称:小鼠Epas1重组蛋白
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货号:CSB-YP007705MO
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规格:
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来源:Yeast
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其他:
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中文名称:小鼠Epas1重组蛋白
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货号:CSB-EP007705MO
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规格:
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来源:E.coli
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其他:
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中文名称:小鼠Epas1重组蛋白
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货号:CSB-EP007705MO-B
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规格:
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来源:E.coli
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共轭: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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中文名称:小鼠Epas1重组蛋白
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货号:CSB-BP007705MO
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规格:
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来源:Baculovirus
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其他:
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中文名称:小鼠Epas1重组蛋白
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货号:CSB-MP007705MO
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规格:
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来源:Mammalian cell
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其他:
产品详情
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纯度:>85% (SDS-PAGE)
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基因名:
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Uniprot No.:
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别名:Epas1; Hif2aEndothelial PAS domain-containing protein 1; EPAS-1; HIF-1-alpha-like factor; HLF; mHLF; HIF-related factor; HRF; Hypoxia-inducible factor 2-alpha; HIF-2-alpha; HIF2-alpha
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种属:Mus musculus (Mouse)
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蛋白长度:Partial
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蛋白标签: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. -
产品提供形式: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. -
复溶: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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储存条件:Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保质期: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. -
货期: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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注意事项: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.
靶点详情
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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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基因功能参考文献:
- Increased HIF-2alpha expression is associated with the development of severe pulmonary hypertension. PMID: 29074488
- EPAS1 links DOCK8 deficiency to atopic skin inflammation via IL-31 induction in CD4thorn T cells. PMID: 28067314
- Myeloid-specific deletion of Epas1 had no impact on the number of myeloid cells migrating into the eye. PMID: 28112274
- Defect in nephron formation in PHD2/PHD3 double mutants required intact hypoxia-inducible factor-2 signaling and was dependent on the extent of stromal hypoxia-inducible factor activation. Thus, hypoxia-inducible factor prolyl-4-hydroxylation in renal interstitial cells is critical for normal nephron formation. PMID: 28847650
- Absence of Hif2a in retinal neuroprogenitor cells causes a marked reduction of proliferating endothelial cells at the angiogenic front. This results in delayed retinal vascular development, fewer major retinal vessels and reduced density of the peripheral deep retinal vascular plexus. PMID: 29615467
- HIF2alpha is linked to tumor suppression in neuroblastoma. PMID: 28696319
- HIF-1alpha-dependent, HIF-2alpha-independent angiogenesis and constitutive diuresis is caused by Vhl deletion in renal epithelia PMID: 27528422
- Data show that Tet1 modulates HIF-2alpha and HIF-1alpha through different mechanisms. PMID: 29036334
- intestine HIF-2alpha regulates ceramide metabolism mainly from the salvage pathway, by positively regulating the expression of Neu3, the gene encoding neuraminidase 3. These results suggest that intestinal HIF-2alpha could be a viable target for hepatic steatosis therapy PMID: 29035368
- endothelial EPAS1 has a global protective role during glomerular hypertensive injuries without influencing the hypertensive effect of angiotensin II PMID: 28928136
- findings indicate that HIF-2alpha increases cancer cell growth by up-regulating YAP1 activity PMID: 28848049
- Chronic activity of HIF2 in stromal progenitors impairs kidney development. Finally, these data confirm the concept that normal stroma function is essential for normal tubular differentiation. PMID: 28527294
- this study shows that HIF-2alpha acts in resting macrophages as a phagocytosis suppressor implying an important relationship between the levels of HIF-2alpha and susceptibility to infection PMID: 27671111
- in neurons HIF-1 and HIF-2 have redundant functions for cellular survival under ischemic conditions. By contrast, lack of anti-survival factors in Hif1a/Hif2a-deficient mice might protect from early acute neuronal cell death and neurological impairment, indicating a benefit of HIF-pathway inhibition in neurons in the very acute phase after ischemic stroke PMID: 26746864
- HIF-2alpha is a novel regulator of neutrophil recruitment to colon tumors. PMID: 27956697
- AQP1 deficiency delays long-term ischemia-reperfusion resolution, partly through repressing angiogenesis mediated by destabilizing HIF-2alpha. PMID: 26649797
- HIF1alpha and HIF2alpha are dispensable for muscle stem cell function under normoxia but are required for maintaining satellite cell self-renewal in hypoxic environments. PMID: 28232488
- Data identify endothelial HIF-2 as a key transcription factor in the pathogenesis of pulmonary hypertension. PMID: 26976644
- eIF3e is an angiogenesis suppressor. Silencing of eIF3e promotes blood perfusion recovery after limb ischemia through stabilization of hypoxia-inducible factor 2alpha activity. PMID: 25758454
- The regulatory connection between HIF-2alpha and VEGFR-1, VEGFR-2 and MMP2. PMID: 27075652
- HIF2alpha is essential for the acute postprandial regulation of hepatic glucagon signaling. PMID: 26853750
- demonstrate that HIF-2alpha is clearly implicated in the TSP1 pulmonary regulation and provide new insights on its contribution to pulmonary arterial hypertension-driven vascular remodelling and vasoconstriction PMID: 26503986
- Findings identify a reciprocal activation mechanism involving HIF-2alpha and the zinc-ZIP8-MTF1 axis during osteoarthritis pathogenesis that amplifies catabolic signaling and cartilage destruction. PMID: 26241779
- This review emphasizes that sympathetic nervous system homeostasis is dependent on a balance between HIF-2alpha and HIF-1alpha. PMID: 25953833
- genetic analysis suggests that tubulointerstitial cellular crosstalk modulates renal EPO production under conditions of epithelial HIF activation in the kidney. PMID: 26927670
- Chondrocytes co-cultured with HIF-2alpha-overexpressing fibroblast-like synoviocytes exhibited upregulation of Mmp3 and Mmp13, which is similar to the effects induced by interleukin (IL)-6 treatment of chondrocytes. PMID: 26642431
- HIF-2alpha inhibits high-grade soft tissue sarcoma cell growth. Loss of HIF-2alpha promotes sarcoma proliferation and increases calcium and mTORC1 signalling in undifferentiated pleomorphic sarcoma and dedifferentiated liposarcoma. PMID: 26837714
- HIF-2alpha-deficient mice displayed brown adipose tissue dysregulation, associated with reduced levels of uncoupling protein 1 (UCP1) and a dysfunctional thermogenic response to cold exposure. PMID: 26572826
- Activation of the HIF signaling pathway could be an important pathogenetic event in the development and progression of at least a subset of these tumors. PMID: 26348575
- Loss of Hif-2alpha Rescues the Hif-1alpha Deletion Phenotype of Neonatal Respiratory Distress In Mice PMID: 26422241
- although Hif-1alpha and Hif-2alpha synergize to suppress the development of acute myeloid leukemia, they are not required for leukemic stem cells maintenance. PMID: 26642852
- Letter: HIF2alpha is expressed in a distinct spatial and temporal pattern throughout venous thrombus resolution. PMID: 25087887
- Results show that HIF2-a is up regulated in an in vitro model of nicotine plus lipopolysccharide-stimulated periodontal ligament cell line and primary culture. Its inhibition exhibits anti-inflammatory activity. PMID: 25565665
- High expression of HIF-2A is associated with leukemia and lymphoma. PMID: 25921247
- HIF2alpha has a cardiomyogenesis-promoting effect in embryonic stem cells via enhancing the activation of the Wnt/beta-catenin signaling pathway. PMID: 25889500
- data suggest that targeting intestinal HIF-2alpha has a significant therapeutic potential in SCD pathophysiology PMID: 26296885
- these results suggest that PTEN is required for apoptosis-mediated cavitation during epithelial morphogenesis by regulating the expression of HIF-2alpha and Bnip3 PMID: 25394489
- excess in pancreatic beta-cells does not play a significant role in beta-cell function and glucose homeostasis PMID: 25833250
- details the importance of breast milk iron in neonatal development and uncovers an unexpected molecular mechanism for the regulation of nutritional status of breast milk through intestinal HIF-2alpha PMID: 26124130
- Hif-2alpha activation augments peroxisome turnover by selective autophagy (pexophagy) and thereby changes lipid composition reminiscent of peroxisomal disorders. PMID: 25440060
- pivotal role in the pathogenesis of rheumatoid arthritis by regulating fibroblast-like synoviocyte functions, independent of HIF-1alpha PMID: 24914685
- The PTEN/PI3K/AKT signaling axis controls hypoxia-induced HIF1alpha (HIF1A) and HIF2alpha (EPAS1) stability in macrophages. PMID: 25103499
- Hypoxia-mediated changes in cardiac mitochondrial function are a conserved target of both HIF-dependent and independent signaling pathways. PMID: 24607765
- we showed that muscles did not require macrophagic hif1a or hif2a to regenerate. These results indicate that macrophagic HIFs do not play a crucial role during skeletal muscle regeneration induced by sterile tissue damage. PMID: 25750431
- These results suggest that there is a compensatory pathway involving HIF-1alpha that regulates the expression of some HIF-2alpha target genes. PMID: 25557133
- 713 HIF-1 and 795 HIF-2 binding sites were identified under hypoxia. Pretreatment with IL-10 altered the binding pattern, with 120 new HIF-1 and 188 new HIF-2 binding sites emerging PMID: 25450522
- Chronic activation of HIF-2 in renal juxtaglomerular cells leads to a reprogramming of the cells into fibroblast-like cells resembling native erythropoietin-producing cells located in the tubulointerstitium. PMID: 25071089
- activation of HIF2alpha/VE-PTP signaling via PHD2 inhibition has the potential to prevent the formation of leaky vessels and edema in inflammatory diseases such as ARDS PMID: 25574837
- Hypoxic treatment of primary keratinocytes induced filaggrin (Flg) gene expression in a HIF1alpha- and HIF2alpha-dependent manner. PMID: 24999590
- HIF-2alpha/IGF-1R signal loop supports the proliferation and Oct4 maintenance of mouse germline stem cells. PMID: 24598112
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亚细胞定位:Nucleus. Nucleus speckle.
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组织特异性:Expressed in most tissues, with highest levels in lung, followed by heart, kidney, brain and liver. Predominantly expressed in endothelial cells. Also found in smooth muscle cells of the uterus, neurons, and brown adipose tissue. High expression in embryo
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