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

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中文名稱：

Recombinant Human Hypoxia-inducible factor 1-alpha inhibitor (HIF1AN)
品名簡稱：

Recombinant Human HIF1AN protein
貨號：

CSB-YP865160HUf0
說明書：

MSDS Datasheet
規格：

￥1836
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

純度：

Greater than 95% as determined by SDS-PAGE.
生物活性：

Not Test
基因名：

HIF1AN
Uniprot No.：

Q9NWT6
別名：

Factor inhibiting HIF-1;FIH-1;Hypoxia-inducible factor asparagine hydroxylase
種屬：

Homo sapiens (Human)
蛋白長度：

Full Length of Mature Protein
來源：

Yeast
分子量：

65.8 kDa
表達區域：

2-349aa
氨基酸序列

AATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
蛋白標簽：

C-terminal GST-tagged
產品提供形式：

Liquid or 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.
緩沖液：

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
復溶：

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：

3-7 business days
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Datasheet & COA：

Please contact us to get it.

產品評價

靶點詳情

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.
基因功能參考文獻：
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. Authors 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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亞細胞定位：

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.
數據庫鏈接：

HGNC: 17113

OMIM: 606615

KEGG: hsa:55662

STRING: 9606.ENSP00000299163

UniGene: Hs.500788