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  4. Recombinant Human Hypoxia-inducible factor 1-alpha inhibitor (HIF1AN)

Recombinant Human Hypoxia-inducible factor 1-alpha inhibitor (HIF1AN)

  • 货号：
    CSB-YP865160HU
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP865160HU-B
  • 规格：
  • 来源：
    E.coli
  • 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.

  • 其他：
  • 货号：
    CSB-BP865160HU
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP865160HU
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    HIF1AN
  • Uniprot No.：
  • 别名：
    DKFZp762F1811; Factor inhibiting HIF-1; Factor inhibiting HIF1 ; FIH 1; FIH-1; FIH1; FLJ20615; FLJ22027 ; HIF1AN; HIF1N_HUMAN; Hypoxia inducible factor 1 alpha inhibitor; Hypoxia inducible factor 1 alpha subunit inhibitor; Hypoxia inducible factor asparagine hydroxylase; Hypoxia-inducible factor 1-alpha inhibitor; Hypoxia-inducible factor asparagine hydroxylase; Peptide aspartate beta dioxygenase
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Full Length
  • 表达区域：
    1-349
  • 氨基酸序列
    MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN
  • 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.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 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.
  • 注意事项：
    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.

产品评价

靶点详情

  • 功能：
    Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.
  • 基因功能参考文献：
    1. Since the FIH-1 dependent hydroxylation of NAA10 occurs oxygen-dependently, NAA10 acetylates HIF-1alpha under normoxia but does not under hypoxia. PMID: 30237125
    2. s identified KANK3 as a new substrate for the oxygen sensor hypoxia-inducible factor 1-alpha inhibitor (HIF1AN), which hydroxylates HIF-1/2alpha and other ankyrin repeat domain-containing proteins at asparagine residues. PMID: 29047187
    3. MiR-31-5p plays an important role in HS formation by inhibiting FIH and regulating the HIF-1alpha pathway. PMID: 29056521
    4. Low FIH1 expression is associated with chemotherapy resistance in breast cancer. PMID: 28061479
    5. data support a model in which the facial triad carboxylate Asp(201) provides both steric and polar contacts to favor O2 access to the Fe(II) only after substrate binds, leading to coupled turnover in FIH and other alphaKG oxygenases. PMID: 27815979
    6. None of the clinicopathological parameters were associated with the expressions of FIH-1 and SOCS3 at mRNA level. PMID: 26749281
    7. This study provides novel clues indicating that miR-21, miR-31, and miR-184 co-target FIH tumor suppressor during pathogenesis in the vast majority of head and neck squamous cell carcinoma. PMID: 25351569
    8. Results suggest that NECAB3, a novel Mint3-binding protein, activates HIF-1 to promote normoxic glycolysis and tumorigenicity by forming a ternary complex with Mint3 and FIH-1. PMID: 26948053
    9. OTUB1 is a target for functional hydroxylation by FIH. PMID: 26752685
    10. demonstrates that miR-135b regulates ERalpha, AR and HIF1AN protein levels through interaction with their 3'UTR regions, and proliferation in ERalpha-positive BCa and AR-positive PCa cells PMID: 25907805
    11. Hypoxia, FIH inhibitors and mutation of asparagine 242 all potentiated TRPV3-mediated current, without altering TRPV3 protein levels, indicating that oxygen-dependent hydroxylation inhibits TRPV3 activity. PMID: 25413349
    12. the nuclear entry of FIH-1 depends on HIF-1alpha PMID: 25687434
    13. data support the concept that FIH-1 may interact with Notch2 and repress its activity, thereby playing a critical role in controlling the survival of vascular endothelial cells PMID: 25837583
    14. miR-31/FIH1 pathway associates with liver fibrosis, perhaps by participation in the TGF-beta/Smad3 signalling of hepatic stellate cells. PMID: 25728779
    15. FIH follows the consensus mechanism for alphaKG oxygenases, suggesting that FIH may be an ideal enzyme to directly access steps involved in O2 activation among the broad family of alphaKG oxygenases. PMID: 25423620
    16. The critical role of miR-31/FIH-1 nexus in colorectal cancer (CRC)was revealed and the contribution of miR-31 to CRC development by targeting FIH-1 was clarified. PMID: 24521875
    17. Data indicate that exosomal miR-135b directly suppressed its target factor-inhibiting hypoxia-inducible factor 1 (FIH-1) in endothelial cells. PMID: 25320245
    18. FIH-1 activity does not represent a major mechanism by which NP cells control HIF-1-dependent transcription, a testament to their adaptation to a unique hypoxic niche. PMID: 24867948
    19. The role of FIH-1 in regulating the transcriptional activity of HIF1A in glioblastoma multiforme. PMID: 24465898
    20. The role of FIH expression in high-risk locally advanced renal cell carcinoma (LARCC) was explored. PMID: 24388053
    21. Comparison of the structure of JMJD5 with that of FIH, a well characterized protein hydroxylase, reveals that human JMJD5 might function as a protein hydroxylase. PMID: 24100311
    22. FIH-1 depletion did lead to impaired binding of Par-3 to ASPP2. PMID: 23606740
    23. The stable Fe-OH2 bond plays an important part in FIH1's regulatory role over O2 homeostasis in humans and points toward a strategy for tightly coupling O2 activation with C-terminal transactivation domain of HIF-1alpha hydroxylation. PMID: 23351038
    24. Our results define a previously unknown mechanism for keratinocyte fate decisions where Notch signaling potential is, in part, controlled through a miR-31/FIH-1 nexus. PMID: 22891326
    25. Glycogen regulation in a HIF-1alpha-independent manner is a novel function for FIH-1 and provides new insight into how the corneal epithelium regulates its energy requirements. PMID: 22532441
    26. FIH activity is essential for tumor growth through the suppression of the p53-p21 axis, the major barrier that prevents cancer progression. PMID: 22002313
    27. FIH1 is expressed in the majority of invasive breast carcinomas and shows distinct subcellular localization patterns. PMID: 21732131
    28. Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation. PMID: 21808058
    29. The expression imbalance of HPH1 and FIH-1 in placenta may play an important role in the pathogenesis and development of severe pre-eclampsia through inhibiting HIF-1alpha. PMID: 19134330
    30. FIH does not uncouple O2 during turnover conditions, nor does it release reactive oxygen species under any tested conditions. PMID: 21443853
    31. Data report that histidinyl residues within the ankyrin repeat domain of tankyrase-2 can be hydroxylated by factor-inhibiting hypoxia-inducible factor. PMID: 21251231
    32. FIH also catalyzes the hydroxylation of highly conserved Asn residues within the ubiquitous ankyrin repeat domain (ARD)-containing proteins PMID: 21177872
    33. Bax-mediated apoptosis is suppressed by FIH1 overexpression, but accelerated by FIH1 deficiency. PMID: 21069436
    34. FIH1 appears to be a suppressor of oxygen-dependent genes in the kidney, operating through HIF-dependent and -independent mechanisms. PMID: 20720525
    35. Methylation-induced epigenetic silencing of FIH is unlikely to underlie up-regulated HIF-1alpha expression in human breast cancer but may play a role in other tumour types. PMID: 20727020
    36. miR-31 contributes to the development of head and neck squamous cell carcinoma by impeding FIH to activate HIF under normoxic conditions. PMID: 20145132
    37. Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha PMID: 11959990
    38. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor PMID: 12080085
    39. present the structure of factor-inhibiting HIF-1 (FIH-1); describe the molecular details of the active site architecture mediating Fe(II) and 2-oxoglutarate binding PMID: 12432100
    40. FIH-1 has a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau protein PMID: 12482756
    41. asparaginyl hydroxylase (FIH) catalytic properties in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases PMID: 14701857
    42. Molecular modeling of the HIF-1alpha CAD V802A in complex with FIH-1 predicted an alteration in asparagine positioning providing an explanation for the impaired catalysis, confirming the importance of Val-802 in asparaginyl hydroxylation by FIH-1. PMID: 14734545
    43. Human HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also efficiently hydroxylates specific asparaginyl (Asn)-residues within proteins of the IkappaB family. PMID: 17003112
    44. ARD proteins function as natural inhibitors of FIH and that the hydroxylation status of these proteins provides another oxygen-dependent interface that modulates HIF signaling PMID: 17573339
    45. Data show that in renal cell carcinoma, the Cut-like homeodomain protein is involved in FIH-1 transcriptional regulation and is controlled by a specific signaling event involving protein kinase C zeta. PMID: 17682059
    46. FIH-1 is widely expressed in invasive breast carcinoma. The hypoxic response and survival suggests that tumour regulation of FIH-1 is an additional important mechanism for HIF pathway activation. PMID: 18096060
    47. These results suggest that Siah-1 might play a role as a regulator of FIH abundance under normoxic conditions. PMID: 18280659
    48. FIH-1 hydroxylates Notch ICD at two residues (N(1945) and N(2012)) that are critical for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis PMID: 18299578
    49. two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH) PMID: 18611856
    50. Overexpression of the oxygen sensor FIH1 is associated with tumor aggressiveness in pancreatic endocrine tumors. PMID: 18927305

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  • 亚细胞定位：
    Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.
  • 数据库链接：

    HGNC: 17113

    OMIM: 606615

    KEGG: hsa:55662

    STRING: 9606.ENSP00000299163

    UniGene: Hs.500788