Anti-HIF1 alpha (Hydroxy P564) antibody (ab72777)

Overview

• Product nameAnti-HIF1 alpha (Hydroxy P564) antibodySee all HIF1 alpha primary antibodies ...
• Description
  Rabbit polyclonal to HIF1 alpha (Hydroxy P564)
• SpecificityThis antibody reacts specifically with HIF1 alpha (Hydroxy P564). No cross reactivity was shown with non modified peptide.
• Tested applicationsWB more details
• Species reactivity
  Reacts with: Human
  Predicted to work with: a wide range of other species
• Immunogen

  A 15 residue synthetic peptide derived from human HIF1 alpha containing hydroxyproline at position 564.

Properties

• FormLiquid
• Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
• Storage bufferPreservative: None
  Constituents: Whole serum
• PurityWhole antiserum
• Clonality Polyclonal
• IsotypeIgG
• Research Areas
  • Metabolism
  • Types of disease
  • Cancer

  • Metabolism
  • Pathways and Processes
  • Metabolism processes
  • Hypoxia

  • Metabolism
  • Pathways and Processes
  • Metabolic signaling pathways
  • Nucleotide metabolism

  • Cancer
  • Invasion/microenvironment
  • Hypoxia
  • HIF

  • Cancer
  • Cancer Metabolism
  • Response to hypoxia

  • Cardiovascular
  • Hypoxia
  • HIF

  • Epigenetics and Nuclear Signaling
  • Transcription
  • Domain Families
  • HLH / Leucine Zipper
  • HLH

  • Epigenetics and Nuclear Signaling
  • Cardiovascular/Immune
  • Hypoxia
  • HIF

Applications

Target

• FunctionFunctions 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.
• Tissue specificityExpressed 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.
• Sequence similaritiesContains 1 basic helix-loop-helix (bHLH) domain.
  Contains 1 PAC (PAS-associated C-terminal) domain.
  Contains 2 PAS (PER-ARNT-SIM) domains.
• DomainContains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID).
• Post-translational
  modificationsIn 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. Deubiquitinated by USP20. 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.
  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.
• Cellular localizationCytoplasm. Nucleus. Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia.

Target information above from: UniProt accession Q16665 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 3091 Human
  • Omim: 603348 Human
  • SwissProt: Q16665 Human
  • Unigene: 597216 Human

• Alternative names
  ARNT interacting protein antibodyARNT-interacting protein antibodyBasic helix loop helix PAS protein MOP1 antibody

  Basic-helix-loop-helix-PAS protein MOP1 antibodybHLHe78 antibodyClass E basic helix-loop-helix protein 78 antibodyHIF 1A antibodyHIF 1alpha antibodyHIF-1-alpha antibodyHIF1 A antibodyHIF1 Alpha antibodyHIF1 antibodyHIF1-alpha antibodyHIF1A antibodyHIF1A_HUMAN antibodyHypoxia inducible factor 1 alpha antibodyHypoxia inducible factor 1 alpha isoform I.3 antibodyHypoxia inducible factor 1 alpha subunit antibodyHypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor antibodyHypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor) antibodyHypoxia inducible factor1alpha antibodyHypoxia-inducible factor 1-alpha antibodyMember of PAS protein 1 antibodyMember of PAS superfamily 1 antibodyMember of the PAS Superfamily 1 antibodyMOP 1 antibodyMOP1 antibodyPAS domain-containing protein 8 antibodyPASD 8 antibodyPASD8 antibody

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