Key features and details
- Rabbit polyclonal to HIF-1 alpha
- Suitable for: IHC-P, WB, ICC/IF, Flow Cyt
- Reacts with: Mouse, Rat, Human
- Isotype: IgG
Product nameAnti-HIF-1 alpha antibody
See all HIF-1 alpha primary antibodies
DescriptionRabbit polyclonal to HIF-1 alpha
Tested applicationsSuitable for: IHC-P, WB, ICC/IF, Flow Cytmore details
Species reactivityReacts with: Mouse, Rat, Human
- IHC-P: Human cervical carcinoma tissue. WB: Mouse heart lysates; rat brain and spleen tissue lysates; HL60 cell lysate. ICC/IF: KLN 205 cells.
HIF-1 alpha can be a difficult target to work with so we have compiled a summary of all the important information you need to know including useful tips. This can be found in the protocols tab or alternatively click here to download the English version and here to download the Mandarin.
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.09% Sodium azide
Constituents: 1% BSA, 50% Glycerol
Concentration information loading...
PurityProtein A purified
Our Abpromise guarantee covers the use of ab216842 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||1/100 - 1/500.|
|WB||1/100 - 1/1000. Detects a band of approximately 92 kDa (predicted molecular weight: 92 kDa).|
|ICC/IF||1/50 - 1/200.|
|Flow Cyt||1/20 - 1/100.|
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).
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.
- Information by UniProt
- ARNT interacting protein antibody
- ARNT-interacting protein antibody
- Basic helix loop helix PAS protein MOP1 antibody
All lanes : Anti-HIF-1 alpha antibody (ab216842) at 1/200 dilution
Lane 1 : Mouse heart lysate
Lane 2 : Mouse large intestine lysate
All lanes : Goat anti-rabbit IgG antibody (H+L), HRP at 1/3000 dilution
Predicted band size: 92 kDa
Immunohistochemical analysis of formalin-fixed, paraffin-embedded human cervical carcinoma tissue labeling HIF-1-alpha with ab216842 at 1/300 dilution followed by conjugation to the secondary antibody and DAB staining.
Immunofluorescent analysis of KLN 205 (mouse) cells labeling HIF-1-alpha with ab216842 at 1/50 dilution followed by an FITC conjugated secondary antibody.
All lanes : Anti-HIF-1 alpha antibody (ab216842) at 1/1000 dilution
Lanes 1-2 : Rat spleen tissue lysate
Lane 3 : Rat brain tissue lysate
Lane 4 : Rat brain tissue lysate
Predicted band size: 92 kDa
Anti-HIF-1 alpha antibody (ab216842) at 1/300 dilution + HL60 cell lysate
Goat Anti-Rabbit IgG Antibody (H+L), HRP at 1/5000 dilution
Predicted band size: 92 kDa
Flow Cytometry analysis of HeLa (Human epithelial cell line from cervix adenocarcinoma) cells, labeling HIF-1 aplha with ab216842 at a 1/100 dilution for 30 minutes (green) compared to control cells (blue) and an isotype control (orange).
ab216842 has been referenced in 12 publications.
- Chen X et al. Salidroside ameliorated hypoxia-induced tumorigenesis of BxPC-3 cells via downregulating hypoxia-inducible factor (HIF)-1a and LOXL2. J Cell Biochem 121:165-173 (2020). PubMed: 31162697
- Jing L et al. Protective effects of two novel nitronyl nitroxide radicals on heart failure induced by hypobaric hypoxia. Life Sci 248:116481 (2020). PubMed: 31102744
- Xu J et al. HIF1a overexpression enhances diabetic wound closure in high glucose and low oxygen conditions by promoting adipose-derived stem cell paracrine function and survival. Stem Cell Res Ther 11:148 (2020). PubMed: 32248837
- Yu H et al. Expression of HIF-1a in cycling stretch-induced osteogenic differentiation of bone mesenchymal stem cells. Mol Med Rep 20:4489-4498 (2019). PubMed: 31702030
- Zhang T et al. LncRNA AWPPH promotes the invasion and migration of glioma cells through the upregulation of HIF1a. Oncol Lett 18:6781-6786 (2019). PubMed: 31807187