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04-1006 Anti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal

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      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, RWB, ICC, IH(P)RbUnpurifiedMonoclonal Antibody
      Catalogue Number04-1006
      DescriptionAnti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal
      Alternate Names
      • ARNT interacting protein
      • ARNT-interacting protein
      • Basic-helix-loop-helix-PAS protein MOP1
      • HIF-1 alpha
      • HIF1 alpha, member of PAS protein 1
      • hypoxia inducible factor 1
      Background InformationHypoxia, a condition of low tissue O2 concentration, plays an important role in normal physiological processes and tumor formation. Under hypoxic conditions mammalian cells up regulate the expression of hypoxic genes, including induction of angiogenesis and a switch to anaerobic metabolism, in order to survive. HIF-1 (Hypoxia Inducible Factor-1) is one of the key regulators of the transcriptional response to oxygen deprivation (1). HIF-1 is composed of two subunits, HIF-1αand HIF-1β also known as aryl hydrocarbon receptor nuclear translocator (ARNT)) that are members of the basic helix-loop-helix (bHLH) Per-Arnt-Sim (PAS) (bHLH-PAS) family of transcription factors. HIF-1 is essential for angiogenesis, embryonic development, and is associated with tumor progression, erythropoiesis, vascular development/remodeling, vasodilation, and glucose/energy metabolism. The over expression of HIF-1αhas been demonstrated in many common human cancers including prostate and breast, in which HIF-1α levels are associated with increase vascularitry and tumor progression. Besides physiological hypoxia, genetic abnormalities frequently detected in human cancers, such as loss of function mutations (Von Hippel-Lindau, p53, and PTEN), are associated with induction of HIF1 activity and expression of HIF-1-inducible genes (1).
      Product Information
      HS Code3822 00 90
      • Ramos + CoCl2 lysate
      PresentationRabbit Monoclonal in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl containing 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
      ApplicationPlease note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target.
      Key Applications
      • Western Blotting
      • Immunocytochemistry
      • Immunohistochemistry (Paraffin)
      Application NotesImmunohistochemistry Analysis: A 1:100-250 dilution from a previous lot detected HIF-1α in human liver carcinoma tissue.
      Immunocytochemistry Analysis: A 1:100-250 dilution from a previous lot was used in IC.
      Biological Information
      ImmunogenSynthetic peptide corresponding to residues near the C-terminus of human HIF-1α.
      SpecificityThis antibody recognizes HIF-1α at and around the C-terminus.
      Species Reactivity
      • Human
      • Rat
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Gene Symbol
      • HIF-1alpha
      • HIF1
      • HIF1-ALPHA
      • MOP1
      • PASD8
      • bHLHe78
      Purification MethodUnpurified
      UniProt Number
      UniProt SummaryFUNCTION: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP.
      SUBUNIT STRUCTURE: Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability By similarity. Interacts with CREBBP and EP300 (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10 By similarity.
      SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia.
      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.
      INDUCTION: Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF FGF-2 FGF-2 IGF-2, TGF-1 beta, HGF, TNF alpha, IL-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia.
      DOMAIN: Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID).
      PTM: In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD1 and EGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization.
      In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol.
      S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.
      Requires phosphorylation for DNA-binding.
      Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity By similarity.
      Ubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-532 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-803.
      The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.
      SEQUENCE SIMILARITIES: Contains 1 basic helix-loop-helix (bHLH) domain.
      Contains 1 PAC (PAS-associated C-terminal) domain.
      Contains 2 PAS (PER-ARNT-SIM) domains.
      Molecular Weight~120 kDa
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Western Blot on Ramos + CoCl2 lysates.
      Western Blot Analysis: A 1:2,000 dilution of this antibody was used to detect HIF-1α in Ramos + CoCl2 lysate.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at -20ºC from date of receipt. Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information
      Global Trade Item Number
      Catalogue Number GTIN
      04-1006 04053252677182


      Anti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal MSDS


      Safety Data Sheet (SDS) 

      Anti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal Certificates of Analysis

      TitleLot Number
      Anti-HIF-1#945;, clone EP1215Y, Rabbit Monoclonal - 2022629 2022629
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 1996257 1996257
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2021747 2021747
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2022055 2022055
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2034730 2034730
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2073094 2073094
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2161248 2161248
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - 2324382 2324382
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - JBC1787367 JBC1787367
      Anti-HIF-1, clone EP1215Y, Rabbit Monoclonal - NG1628017 NG1628017


      Reference overviewApplicationPub Med ID
      The tyrosine phosphatase SHP-1 regulates hypoxia inducible factor-1α (HIF-1α) protein levels in endothelial cells under hypoxia.
      Alig, SK; Stampnik, Y; Pircher, J; Rotter, R; Gaitzsch, E; Ribeiro, A; Wörnle, M; Krötz, F; Mannell, H
      PloS one  10  e0121113  2015

      Show Abstract
      25799543 25799543
      Hypoxia-inducible factor 1 contributes to N-acetylcysteine's protection in stroke.
      Zhang, Z; Yan, J; Taheri, S; Liu, KJ; Shi, H
      Free radical biology & medicine  68  8-21  2014

      Show Abstract
      24296245 24296245
      The role of hypoxia-inducible factor-1α and vascular endothelial growth factor in late-phase preconditioning with xenon, isoflurane and levosimendan in rat cardiomyocytes.
      Goetzenich, A; Hatam, N; Preuss, S; Moza, A; Bleilevens, C; Roehl, AB; Autschbach, R; Bernhagen, J; Stoppe, C
      Interactive cardiovascular and thoracic surgery  18  321-8  2014

      Show Abstract
      Western Blotting24351506 24351506
      Ischemia induces different levels of hypoxia inducible factor-1α protein expression in interneurons and pyramidal neurons.
      Ramamoorthy, P; Shi, H
      Acta neuropathologica communications  2  51  2014

      Show Abstract
      Immunofluorescence24887017 24887017
      Differential effects of HIF-1 inhibition by YC-1 on the overall outcome and blood-brain barrier damage in a rat model of ischemic stroke.
      Yan, J; Zhou, B; Taheri, S; Shi, H
      PloS one  6  e27798  2011

      Show Abstract
      22110762 22110762

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      Life Science Research > Antibodies and Assays > Primary Antibodies