The antiserum was produced against synthesized peptide derived from human HIF-1alpha. AA range:328-377

HIF-1α Polyclonal Antibody detects endogenous levels of HIF-1α protein.

HIF1A

Hypoxia-inducible factor 1-alpha

HIF1A ;
BHLHE78 ;
MOP1 ;
PASD8 ;
Hypoxia-inducible factor 1-alpha ;
HIF-1-alpha ;
HIF1-alpha ;
ARNT-interacting protein ;
Basic-helix-loop-helix-PAS protein MOP1 ;
Class E basic helix-loop-helix protein 78 ;
bHLHe78 ;
Member of PAS protein 1 ;
PAS doma

hypoxia inducible factor 1 alpha subunit (HIF1A) Homo sapiens This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1) , which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes , including those involved in energy metabolism , angiogenesis , apoptosis , and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in embryonic vascularization , tumor angiogenesis and pathophysiology of ischemic disease. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq , Jul 2011] ,

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) . ,Function: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. ,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. ,online information:Hypoxia inducible factor entry ,PTM: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. ,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. ,PTM:Requires phosphorylation for DNA-binding. ,PTM:S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex. ,PTM:Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity. ,PTM:The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. ,PTM: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. ,similarity:Contains 1 basic helix-loop-helix (bHLH) domain. ,similarity:Contains 1 PAC (PAS-associated C-terminal) domain. ,similarity:Contains 2 PAS (PER-ARNT-SIM) domains. ,subcellular location:Cytoplasmic in normoxia , nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus , under hypoxia. ,subunit: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. ,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. ,

Cytoplasm . Nucleus . Nucleus speckle . Colocalizes with HIF3A in the nucleus and speckles (By similarity) . Cytoplasmic in normoxia , nuclear translocation in response to hypoxia (PubMed:9822602) . .

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