Anti-HIF1 alpha antibody [H1alpha67] - BSA and Azide free (ab80544)
Overview
- Product nameAnti-HIF1 alpha antibody [H1alpha67] - BSA and Azide freeSee all HIF1 alpha primary antibodies ...
- DescriptionMouse monoclonal [H1alpha67] to HIF1 alpha - BSA and Azide free
- Tested applicationsIHC-P more details
- Species reactivityReacts with: Mouse, Rat, Sheep, Human, Ferret
- Immunogen
Recombinant fragment, corresponding to amino acids 432-528 of Human HIF1 alpha
- Epitopeaa 432-528
- Positive controlMammalian cells cultured under reduced O2 tension.
Properties
- FormLiquid
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: None
Constituents: 10mM PBS, pH 7.4 -
Concentration information loading... - PurityProtein A purified
- Clonality Monoclonal
- Clone numberH1alpha67
- IsotypeIgG2b
- Light chain typekappa
-
Research Areas
Applications
Our Abpromise guarantee covers the use of ab80544 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Notes |
|---|---|
| IHC-P | IHC-P: Use at an assay dependent dilution. |
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.
-
Database links
- Entrez Gene: 3091 Human
- Entrez Gene: 15251 Mouse
- Entrez Gene: 29560 Rat
- Entrez Gene: 443519 Sheep
- Omim: 603348 Human
- SwissProt: Q16665 Human
- SwissProt: Q61221 Mouse
- SwissProt: O35800 Rat
- Unigene: 597216 Human
- Unigene: 3879 Mouse
- Unigene: 446610 Mouse
- Unigene: 10852 Rat
see all
Target information above from: UniProt accession
Q16665
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010)
.
-
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
see all
References for Anti-HIF1 alpha antibody [H1alpha67] - BSA and Azide free (ab80544)
This product has been referenced in:
- Acs G et al. Hypoxia-inducible erythropoietin signaling in squamous dysplasia and squamous cell carcinoma of the uterine cervix and its potential role in cervical carcinogenesis and tumor progression. Am J Pathol 162:1789-806 (2003). IHC-P . Read more (PubMed: 12759237) »