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Mouse Monoclonal HIF-1alpha antibody [1A3] (STJ98135)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, IF, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:200-1:1000; IF 1:200-1:1000; ELISA 1:10000
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
HIF1A antibody, BHLHE78 antibody, MOP1 antibody, PASD8 antibody,|ARNT interacting protein antibody|ARNT-interacting protein antibody|Basic helix loop helix PAS protein MOP1 antibody|Basic-helix-loop-helix-PAS protein MOP1 antibody|bHLHe78 antibody|Class E basic helix-loop-helix protein 78 antibody|HIF 1A antibody|HIF 1alpha antibody|HIF-1-alpha antibody|HIF1 A antibody|HIF1 Alpha antibody|HIF1 antibody|HIF1-alpha antibody|HIF1A antibody|HIF1A_HUMAN antibody|Hypoxia inducible factor 1 alpha antibody|Hypoxia inducible factor 1 alpha isoform I.3 antibody|Hypoxia inducible factor 1 alpha subunit antibody|Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor antibody|Hypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor) antibody|Hypoxia inducible factor1alpha antibody|Hypoxia-inducible factor 1-alpha antibody|Member of PAS protein 1 antibody|Member of PAS superfamily 1 antibody|Member of the PAS Superfamily 1 antibody|MOP 1 antibody|MOP1 antibody|PAS domain-containing protein 8 antibody|PASD 8 antibody|PASD8 antibody|Anti-HIF-1 alpha antibody [H1alpha67] – ChIP Grade (ab1)
SCBT cat No: sc-13515|sc-71247|sc-8711|sc-53546|sc-10790|sc-12542|
HIF-1alpha Monoclonal Antibody
|Catalogue No.|| |
Human, Mouse, Monkey
HIF-1alpha Monoclonal Antibody detects endogenous levels of HIF-1alpha protein.
Purified recombinant fragment of human HIF-1alpha expressed in E Coli
WB, IHC, IF, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:200-1:1000; IF 1:200-1:1000; ELISA 1:10000
HIF-1alpha Antibody was tube-contained. Ascitic fluid containing 0.03% sodium azide.
HIF-1alpha Antibody was purified using affinity purification.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Hypoxia-inducible factor 1-alpha antibody, HIF-1-alpha antibody, HIF1-alpha antibody, ARNT-interacting protein antibody, Basic-helix-loop-helix-PAS protein MOP1 antibody, Class E basic helix-loop-helix protein 78 antibody, bHLHe78 antibody, Member of PAS protein 1 antibody, PAS domain-containing protein 8 antibody
|Protein names|| |
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 domain-containing protein 8
|Protein 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, HILPDA, 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. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.
|Protein 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. A higher level expression seen in pituitary tumors as compared to the pituitary gland.
|Protein sequence and 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). / Contains 1 bHLH (basic helix-loop-helix) domain. / Contains 1 PAC (PAS-associated C-terminal) domain. / Contains 2 PAS (PER-ARNT-SIM) domains.
|Protein post-translational modifications|| |
In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1. 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. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding. Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome. / Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia. Sumoylation can promote either its stabilization or its VHL-dependent degradation by promoting hydroxyproline-independent HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination and proteasomal degradation. Desumoylation by SENP1 increases its stability amd transcriptional activity. There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity. / Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation . Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation . / Polyubiquitinated; 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. Ubiquitinated by a CUL2-based E3 ligase. / The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.
|Protein cellular localization|| |
Cytoplasm / Nucleus / Nucleus speckle
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St John’s Laboratory Ltd.
|Product type|| |
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