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  4. Recombinant Mouse Egl nine homolog 1 (Egln1)

Recombinant Mouse Egl nine homolog 1 (Egln1)

  • 中文名稱：
    小鼠Egln1重組蛋白
  • 貨號：
    CSB-YP821019MO
  • 規(guī)格：
  • 來源：
    Yeast
  • 其他：
  • 中文名稱：
    小鼠Egln1重組蛋白
  • 貨號：
    CSB-EP821019MO
  • 規(guī)格：
  • 來源：
    E.coli
  • 其他：
  • 中文名稱：
    小鼠Egln1重組蛋白
  • 貨號：
    CSB-EP821019MO-B
  • 規(guī)格：
  • 來源：
    E.coli
  • 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.

  • 其他：
  • 中文名稱：
    小鼠Egln1重組蛋白
  • 貨號：
    CSB-BP821019MO
  • 規(guī)格：
  • 來源：
    Baculovirus
  • 其他：
  • 中文名稱：
    小鼠Egln1重組蛋白
  • 貨號：
    CSB-MP821019MO
  • 規(guī)格：
  • 來源：
    Mammalian cell
  • 其他：

產(chǎn)品詳情

  • 純度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 別名：
    Egln1Egl nine homolog 1; EC 1.14.11.29; Hypoxia-inducible factor prolyl hydroxylase 2; HIF-PH2; HIF-prolyl hydroxylase 2; HPH-2; Prolyl hydroxylase domain-containing protein 2; PHD2; SM-20
  • 種屬：
    Mus musculus (Mouse)
  • 蛋白長度：
    Full Length of Mature Protein
  • 表達(dá)區(qū)域：
    2-400
  • 氨基酸序列
    ASDSGGPGV LSASERDRQY CELCGKMENL LRCGRCRSSF YCCKEHQRQD WKKHKLVCQG GEAPRAQPAP AQPRVAPPPG GAPGAARAGG AARRGDSAAA SRVPGPEDAA QARSGPGPAE PGSEDPPLSR SPGPERASLC PAGGGPGEAL SPGGGLRPNG QTKPLPALKL ALEYIVPCMN KHGICVVDDF LGRETGQQIG DEVRALHDTG KFTDGQLVSQ KSDSSKDIRG DQITWIEGKE PGCETIGLLM SSMDDLIRHC SGKLGNYRIN GRTKAMVACY PGNGTGYVRH VDNPNGDGRC VTCIYYLNKD WDAKVSGGIL RIFPEGKAQF ADIEPKFDRL LFFWSDRRNP HEVQPAYATR YAITVWYFDA DERARAKVKY LTGEKGVRVE LKPNSVSKDV
  • 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.
  • 儲存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 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.
  • 注意事項(xiàng)：
    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.

產(chǎn)品評價(jià)

靶點(diǎn)詳情

  • 功能：
    Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
  • 基因功能參考文獻(xiàn)：
    1. Data show that deletion of prolyl hydroxylase 2 (PHD2) in intestinal epithelial cells (IECs) did not lead to spontaneous enteritis or colitis in mice. PMID: 29688249
    2. PHD2 and PHD3 are essential for normal kidney development as the combined inactivation of stromal PHD2 and PHD3 resulted in renal failure that was associated with reduced kidney size, decreased numbers of glomeruli, and abnormal postnatal nephron formation. PMID: 28847650
    3. aberrant hypoxic responses due to dysfunction of PHD2 caused both glomerular and tubular damages in HFD-induced obese mice. Phd2-inactivation provides a novel strategy against obesity-induced kidney injury PMID: 27827416
    4. the expression of PHD2 in endothelial cells plays a critical role in renal fibrosis and vascular remodelling in adult mice. PMID: 28266128
    5. Phd2 expressed in chondrocytes inhibits endochondral ossification at the epiphysis by suppressing HIF signaling pathways. PMID: 27775044
    6. brain tissue protection and increased angiogenesis upon sub-acute ischemic stroke was completely absent in Phd2 knockout mice that were additionally deficient for both Hif1a and Hif2a PMID: 27001147
    7. expression of PHD2 in endothelial cells plays a critical role in preventing pulmonary arterial remodeling in mice PMID: 27613846
    8. PHD-2 knockdown mesenchymal stromal cells overexpressed HIF-1alpha and multiple angiogenic factors compared to control. Wounds treated with PHD-2 knockdown mesenchymal stromal cells healed at a significantly accelerated rate compared with wounds treated with shScramble mesenchymal stromal cells. PMID: 29280872
    9. data identify the PHD2:HIF-2alpha:EPO axis as a so far unknown regulator of osteohematology by controlling bone homeostasis. PMID: 27082941
    10. miR-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating HIF-1alpha/VEGF pathway. PMID: 27030384
    11. Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen stores is linked to the resolution of neutrophil-mediated inflammatory responses PMID: 28805660
    12. Epo transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3, oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity. PMID: 27683416
    13. Notch ligand genes Jag1, Jag2, and Dll1 and target Hes1 became downregulated upon aging HIF-2alpha dependently. PMID: 27821476
    14. Results identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function. PMID: 27795296
    15. Results found that loss of endothelial PHD2 induced pulmonary arterial hypertension and vascular remodeling in a HIF-2-dependent fashion. PMID: 26976644
    16. This study demonstrated that the Neuronal prolyl-4-hydroxylase 2 deficiency improves cognitive abilities in a murine model of cerebral hypoperfusion. PMID: 27720797
    17. We conclude that the activation of the HIF pathway induced by PHD2 deficiency enhances the effect of running training PMID: 27393382
    18. deleting Phd1-3 genes in osteoblasts increased osteoclast formation in vitro and in bone. PMID: 27614241
    19. Key messages: HIF-P4H-2 deficiency protects skeletal muscle from ischemia-reperfusion injury. The mechanisms involved are mediated via normoxic HIF-1alpha and HIF-2alpha stabilization. HIF-P4H-2 deficiency increases capillary size but not number. HIF-P4H-2 deficiency maintains energy metabolism during ischemia-reperfusion. PMID: 26452676
    20. Diminished degradation of FLNA upon PHD2 inactivation in hypoxia rearranges the actin cytoskeleton to reduce the number of dendritic spines, synapses. PMID: 26972007
    21. Stabilized HIF-1alpha induced by PHD2 conditional knockout resulted in the transition of muscle fibers toward a slow fiber type via a calcineurin/NFATc1 signaling pathway. PMID: 26949511
    22. HIF-P4H-2 inhibition may be a novel strategy for protecting against the development of atherosclerosis. PMID: 26848160
    23. findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF) activation; this reversion is associated with loss of matrix stiffening and consequently reduction in spontaneous metastases to lungs and liver PMID: 26323721
    24. Data (including data from studies in transgenic/knockout mice) suggest that expression of Phd2/Egln1 in chondrocytes plays key role in chondrogenesis, osteogenesis, and developmental gene expression regulation. PMID: 26562260
    25. a genetic link between EGLN1 and VWF in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported. PMID: 26047609
    26. results suggest that HLV delivery of shPHD2 might become a promising treatment strategy to promote vascular regeneration in critical limb ischemia disease via enhancing innate endogenous pathways PMID: 25832622
    27. PHD2 in the liver has a role in survival in lactic acidosis by activating the Cori cycle PMID: 26324945
    28. Regulatory link was discovered between mitochondrial Txnrd and the JNK-PHD2-Hif-1alpha axis, which highlights how the loss of Txnrd2 and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis. PMID: 25647640
    29. combined deletion of Phd2 and Phd3 dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury PMID: 26075818
    30. PHD2 activity is a critical contributor to the high fat-diet-induced cardiac dysfunction. PMID: 25546437
    31. Phd2 plays an important role in regulating bone formation in part by modulating expression of Osx and bone formation marker genes. PMID: 24753072
    32. Hif-p4h-2-deficient mice, whether fed normal chow or a high-fat diet, had less adipose tissue, smaller adipocytes, and less adipose tissue inflammation than their littermates. PMID: 24789921
    33. PHD2 silencing through siRNA treatment not only increased the expression of HIF1alpha and VEGFa, but also improved fibroblast proliferation leading to improvement in diabetic wound healing. PMID: 24376825
    34. High PHD2 expression is associated with tumor development. PMID: 23913502
    35. These studies formally prove that a missense mutation in PHD2 is the cause of the erythrocytosis, show that this occurs through haploinsufficiency, and point to multifactorial control of red cell mass by PHD2. PMID: 24121508
    36. Heterozygous inactivation of the enzyme PHD2 is associated with markedly enhanced ventilatory sensitivity to hypoxia. PMID: 23690557
    37. Phd2 deletion in myeloid lineage attenuates hypertensive cardiovascular hypertrophy and fibrosis, which may be mediated by decreased inflammation- and fibrosis-associated gene expression in macrophages PMID: 23778187
    38. Phd2 downregulation by ANG1 promotes proarteriogenic macrophages. PMID: 23616286
    39. Egln1 deficiency only in keratinocytes and not in myeloid or endothelial cells was found to lead to faster wound closure, which involved enhanced migration of the hyperproliferating epithelium. PMID: 23798557
    40. Prolyl hydroxylase domain protein 2 plays a critical role in diet-induced obesity and glucose intolerance. PMID: 23630130
    41. Conditional loss of PHD2 in mice leads to HIF-2alpha-dependent erythrocytosis, whereas HIF-1alpha protects these mice. PMID: 23264599
    42. Neuron-specific prolyl-4-hydroxylase domain 2 knockout reduces brain injury after transient cerebral ischemia. PMID: 22933585
    43. Alterations in the function of all 3 isoforms of prolyl-4-hydroxylase enzymes (PHD1-3) in the first 24 h following transient focal cerebral ischaemia are reported. PMID: 22615432
    44. Data show it is feasible to reactivate hepatic erythropoietin production using systemically delivered siRNAs targeting the EglN1, EglN2 and EglN3 prolyl hydroxylase mRNA specifically in the liver. PMID: 22611156
    45. This study shows that inhibiting prolyl hydroxylase domain 2 increases the hepatocarcinogenesis and stimulates the development of cholangiocarcinoma. PMID: 22420978
    46. PHD2 inhibition is essential for the regulation of the anti-tumoral activity in mouse tumor cells and might bring some new insight in our understanding of tumor growth inhibition. PMID: 22354010
    47. results unravel how PHD2 regulates arteriogenesis and artery homeostasis by controlling a specific differentiation state in macrophages and suggest new treatment options for ischaemic disorders PMID: 21983962
    48. PHD2 mediates oxygen-induced retinopathy in neonatal mice PMID: 21435465
    49. Cardiomyocyte-specific prolyl-4-hydroxylase domain 2 knock out protects from acute myocardial ischemic injury. PMID: 21270129
    50. the underlying mechanism by which ET-1, through the regulation of PHD2, controls HIF-1alpha stability and thereby regulates angiogenesis and melanoma cell invasion PMID: 20574527

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  • 亞細(xì)胞定位：
    Cytoplasm. Nucleus.
  • 組織特異性：
    Expressed in heart, brain liver, skeletal muscle and kidney. Low levels were detected in the lung. Constitutively expressed during differentiation of C2C12 skeletal myocytes.
  • 數(shù)據(jù)庫鏈接：