ARNT interacting protein; ARNT-interacting protein; Basic helix loop helix PAS protein MOP1; Basic-helix-loop-helix-PAS protein MOP1; bHLHe78; Class E basic helix-loop-helix protein 78; HIF 1A; HIF 1alpha; HIF-1-alpha; HIF1 A; HIF1 Alpha; HIF1; HIF1-alpha; HIF1A; HIF1A_HUMAN; Hypoxia inducible factor 1 alpha; Hypoxia inducible factor 1 alpha isoform I.3; Hypoxia inducible factor 1 alpha subunit; Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor; Hypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor); Hypoxia inducible factor1alpha; Hypoxia-inducible factor 1-alpha; Hypoxia-inducible factor-1a; Member of PAS protein 1; Member of PAS superfamily 1; Member of the PAS Superfamily 1; MOP 1; MOP1; PAS domain-containing protein 8; PASD 8; PASD8.
Specific References (22) | bs-0737R has been referenced in 22 publications.
[IF=5.595] Liu T et al. MicroRNA-493 targets STMN-1 and promotes hypoxia-induced epithelial cell cycle arrest in G/M and renal fibrosis. (2018) FASEB J. Sep 05 WB ; Mouse.
[IF=4.91] Fan, Shengjun, et al. "Opposite angiogenic outcome of curcumin against ischemia and Lewis lung cancer models:in silico, in vitro and in vivo studies." Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease (2014). WB ; Mouse.
[IF=4.556] Yang X et al. Synthesis and bioevaluation of novel 18FDG-conjugated 2-nitroimidazole derivatives for tumor-hypoxia imaging. Mol Pharm. 2019 May 6;16(5):2118-2128. IHC&IF ; Mouse&Human.
[IF=4.539] Talwar H et al. MEK2 Negatively Regulates Lipopolysaccharide-Mediated IL-1β Production through HIF-1α Expression. J Immunol. 2019 Mar 15;202(6):1815-1825. WB&IP ; Mouse.
[IF=4.44] Madka, Venkateshwar, et al. "Targeting mTOR and p53 signaling inhibits muscle invasive bladder cancer in vivo." Cancer Prevention Research 9.1 (2016): 53-62. IHC-P ; Mouse.
[IF=3.743] Wang D et al. Effects of hypoxia and ASIC3 on nucleus pulposus cells: From cell behavior to molecularmechanism. Biomed Pharmacother. 2019 Jun 12;117:109061. WB ; Rabbit.
[IF=3.53] Woolf, Eric C., et al. "The Ketogenic Diet Alters the Hypoxic Response and Affects Expression of Proteins Associated with Angiogenesis, Invasive Potential and Vascular Permeability in a Mouse Glioma Model." PLOS ONE10.6 (2015): e0130357. WB ; Mouse.
[IF=3.288] Chai D et al. β2-microglobulin has a different regulatory molecular mechanism between ER+ and ER- breast cancer with HER2.BMC Cancer. 2019 Mar 12;19(1):223. IHC-P ; Human.
[IF=2.989] Ju X et al. Catalpol Promotes the Survival and VEGF Secretion of Bone Marrow-Derived Stem Cells and Their Role in Myocardial Repair After Myocardial Infarction in Rats.Cardiovasc Toxicol. 2018 May 11. WB ; Rat.
[IF=2.91] Shou, Zhu, et al. "Expression and prognosis of FOXO3a and HIF-1?? in nasopharyngeal carcinoma."Journal of cancer research and clinical oncology 138.4 (2012): 585-593.. WB ; Human.
[IF=2.784] Yang D et al. Normobaric oxygen inhibits AQP4 and NHE1 expression in experimental focal ischemic stroke. (2018) Int. J. Mol. Med. WB ; Rat .
[IF=2.566] Yang Z et al. Tenascin-C is involved in promotion of cancer stemness via the Akt/HIF1ɑ axis in esophageal squamous cell carcinoma.Exp Mol Pathol. 2019 Mar 20. WB ; Human.
[IF=2.49] Yang, Ya, et al. "Expression of RAP1B is associated with poor prognosis and promotes an aggressive phenotype in gastric cancer." Oncology reports 34.5 (2015): 2385-2394. IHC-P ; Human.
[IF=1.64] Guo, Wei, et al. "Transplantation of endothelial progenitor cells in treating rats with IgA nephropathy." BMC Nephrology 15.1 (2014): 110. WB ; Rat.
[IF=1.55] Yang, Jinjiang, Ying Lu, and Ai Guo. "Platelet-rich plasma protects rat chondrocytes from interleukin-1β-induced apoptosis." Molecular Medicine Reports 14.5 (2016): 4075-4082. WB ; Rat.
[IF=1.41] Song et al. Effects of HSYA on the proliferation and apoptosis of MSCs exposed to hypoxic and serum deprivation conditions. (2018) Exp.Ther.Med. 15:5251-5260 WB ; Rat.
[IF=.5] Talwar, Harvinder, et al. "The dataset describes: HIF-1 α expression and LPS mediated cytokine production in MKP-1 deficient bone marrow derived murine macrophages." Data in Brief (2017). WB ; Mouse.
[IF=0] Talwar et al. The dataset describes: HIF-1 α expression and LPS mediated cytokine production in MKP-1 deficient bone marrow derived murine macrophages. (2017) Data.Brie. 14:56-61 WB ; Mouse.
[IF=3.414] Li ZH et al. You-Gui-Yin improved the reproductive dysfunction of male rats with chronic kidney disease via regulating the HIF1α-STAT5 pathway. J Ethnopharmacol. 2020 Jan 10;246:112240. WB ; Rat.
WB=1:500-2000 ELISA=1:500-1000 IHC-P=1:100-500 IHC-F=1:100-500 Flow-Cyt=1μg/Test ICC=1:100 IF=1:100-500 （石蠟切片需做抗原修復）
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量
92kDa
細胞定位
細胞核 細胞漿
性 狀
Liquid
濃 度
1mg/ml
免 疫 原
KLH conjugated synthetic peptide derived from middle of human HIF-1 Alpha:341-450/826
亞 型
IgG
純化方法
affinity purified by Protein A
儲 存 液
0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存條件
Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Hypoxia-inducible factor-1 (HIF1) is a transcription factor found in mammalian cells cultured under reduced oxygen tension that plays an essential role in cellular and systemic homeostatic responses to hypoxia. HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator(ARNT). This gene encodes the alpha subunit of HIF-1. Overexpression of a natural antisense transcript (aHIF) of this gene has been shown to be associated with nonpapillary renal carcinomas. Two alternative transcripts encoding different isoforms have been identified.
Function:
Functions as a master transcriptional regulator of theadaptive response to hypoxia. Under hypoxic conditions activatesthe transcription of over 40 genes, including, erythropoietin,glucose transporters, glycolytic enzymes, vascular endothelialgrowth factor, and other genes whose protein products increaseoxygen delivery or facilitate metabolic adaptation to hypoxia.Plays an essential role in embryonic vascularization, tumorangiogenesis and pathophysiology of ischemic disease. Binds to coreDNA sequence 5'-[AG]CGTG-3' within the hypoxia response element(HRE) of target gene promoters. Activation requires recruitment oftranscriptional coactivators such as CREBPB and EP300. Activity isenhanced by interaction with both, NCOA1 or NCOA2. Interaction withredox regulatory protein APEX seems to activate CTAD andpotentiates activation by NCOA1 and CREBBP.
Subunit:
Interacts with COPS5 subunit of COP9 signalosome complex,leading to the regulation of its stability. Interacts with TSGA10(By similarity). Efficient DNA binding requires heterodimerizationof an alpha and a beta/ARNT subunit. Binds to the TAZ-type 1domains of CREBBP and EP300. Interacts with NCOA1, NCOA2, APEX andHSP90. Interacts with VHL which docks HFA1 to the E3 ubiquitinligase complex for subsequent destruction. Interaction, via the ODDdomain, with the beta domain of VHLL, protects HIF1A fromdestruction by competing against the destructive targetinginitiated by VHL.
Subcellular Location:
Cytoplasm. Nucleus.
Tissue Specificity:
Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors.
Post-translational modifications:
In normoxia, is hydroxylated on Pro-402 and Pro-564 in theoxygen-dependent degradation domain (ODD) by EGLN1/PHD1 andEGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564.The hydroxylated prolines promote interaction with VHL, initiatingrapid ubiquitination and subsequent proteasomal degradation. Underhypoxia, proline hydroxylation is impaired and ubiquitination isattenuated, resulting in stabilization.
In normoxia, is hydroxylated on Asn-803 by HIF1AN, thusabrogating interaction with CREBBP and EP300 and preventingtranscriptional activation.
S-nitrosylation of Cys-800 may be responsible for increasedrecruitment of p300 coactivator necessary for transcriptionalactivity of HIF-1 complex.
Acetylation of Lys-532 by ARD1 increases interaction with VHLand stimulates subsequent proteasomal degradation.
Requires phosphorylation for DNA-binding.
Sample:
Lane 1: Hela (Human) Cell Lysate at 30 ug
Lane 2: A431 (Human) Cell Lysate at 30 ug
Lane 3: U251 (Human) Cell Lysate at 30 ug
Lane 4: HepG2 (Human) Cell Lysate at 30 ug
Primary: Anti-HIF-1 Alpha (bs-0737R) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 120 kD
Observed band size: 120 kD
Paraformaldehyde-fixed, paraffin embedded (rat stomach); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30min; Antibody incubation with (HIF-1 Alpha) Polyclonal Antibody, Unconjugated (bs-0737R ) at 1:200 overnight at 4°C, followed by operating according to SP Kit(Rabbit) (sp-0023) instructionsand DAB staining.
Paraformaldehyde-fixed, paraffin embedded (rat kidney); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30min; Antibody incubation with (HIF-1 Alpha) Polyclonal Antibody, Unconjugated (bs-0737R) at 1:200 overnight at 4°C, followed by operating according to SP Kit(Rabbit) (sp-0023) instructionsand DAB staining.
Tissue/cell: human cervical carcinoma; 4% Paraformaldehyde-fixed and paraffin-embedded;
Antigen retrieval: citrate buffer ( 0.01M, pH 6.0 ), Boiling bathing for 15min; Block endogenous peroxidase by 3% Hydrogen peroxide for 30min; Blocking buffer (normal goat serum,C-0005) at 37℃ for 20 min;
Incubation: Anti-HIF-1-Alpha Polyclonal Antibody, Unconjugated(bs-0737R) 1:300, overnight at 4°C, followed by conjugation to the secondary antibody(SP-0023) and DAB(C-0010) staining
Tissue/cell: rat lung tissue(Smoking); 4% Paraformaldehyde-fixed and paraffin-embedded;
Antigen retrieval: citrate buffer ( 0.01M, pH 6.0 ), Boiling bathing for 15min; Block endogenous peroxidase by 3% Hydrogen peroxide for 30min; Blocking buffer (normal goat serum,C-0005) at 37℃ for 20 min;
Incubation: Anti-HIF-1-Alpha Polyclonal Antibody, Unconjugated(bs-0737R) 1:200, overnight at 4°C, followed by conjugation to the secondary antibody(SP-0023) and DAB(C-0010) staining
Hela cell; 4% Paraformaldehyde-fixed; Triton X-100 at room temperature for 20 min; Blocking buffer (normal goat serum, C-0005) at 37°C for 20 min; Antibody incubation with (HIF-1 Alpha) polyclonal Antibody, Unconjugated (bs-0737R) 1:100, 90 minutes at 37°C; followed by a conjugated Goat Anti-Rabbit IgG antibody at 37°C for 90 minutes, DAPI (blue, C02-04002) was used to stain the cell nuclei.
Blank control (blue line): Hela (blue).
Primary Antibody (green line): Rabbit Anti- HIF-1 Alpha antibody (bs-0737R)
Dilution: 1μg /10^6 cells;
Isotype Control Antibody (orange line): Rabbit IgG .
Secondary Antibody (white blue line): Goat anti-rabbit IgG-FITC
Dilution: 1μg /test.
Protocol
The cells were fixed with 80% methanol (5 min at -20℃) and then permeabilized with 0.1% PBS-Tween for 20 min at room temperature. Cells stained with Primary Antibody for 30 min at room temperature. The cells were then incubated in 1 X PBS/2%BSA/10% goat serum to block non-specific protein-protein interactions followed by the antibody for 15 min at room temperature. The secondary antibody used for 40 min at room temperature. Acquisition of 20,000 events was performed.
中文 
暫時沒有說明書
