HIF1 alpha Antibody (YA4893)(PBS only)

Cat. No.: HY-P85201A: Data Sheet User Guide for Antibodies
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HIF1 alpha Antibody (YA4893) is a Rabbit-derived and non-conjugated monoclonal antibody, targeting to HIF1 alpha.

For research use only. We do not sell to patients.

Size		Stock
50 μL		Get quote
100 μL		Get quote

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Documentation

Description

HIF1 alpha Antibody (YA4893) is a Rabbit-derived and non-conjugated monoclonal antibody, targeting to HIF1 alpha.

Host

Rabbit

Molecular Weight

Predicted band size: 93 kDa;

Observed band size: 120 kDa

Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.

Species Reactivity

Human

SwissProt ID

Q16665

Gene ID

3091 [NCBI]

Immunogen

synthetic peptide of human HIF-1-alpha

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:500-1000
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:50-100
IHC-F IHC-F: Immunohistochemistry-Frozen	1:50-100
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:200-500
FC FC: Flow Cytometry	1:500-1:2000
IP IP: Immunoprecipitation	1:50-1:200

Purity	affinity purified.	Conjugation	Non-conjugated
Isotype	IgG

Appearance

Liquid

Formulation

Supplied in PBS, pH 7.4.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Background

Function：Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). 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 (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (PubMed:22009797). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300 (PubMed:16543236, PubMed:9887100). Activity is enhanced by interaction with NCOA1 and/or NCOA2 (PubMed:10594042). Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP (PubMed:10202154, PubMed:10594042). Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (PubMed:19528298); (Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent pro-inflammatory state (PubMed:32697943). In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons (PubMed:32697943). Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response (PubMed:32697943)

Subcellular Localization：Cytoplasm; Nucleus; Nucleus speckle

Expression：
Tissue_specificity:This gene is expressed in most tissues, with the highest expression levels in the kidneys and heart. Due to intratumoral hypoxia and mutations encoding oncoproteins and tumor suppressor genes, this gene is overexpressed in most common human cancers and their metastases. Compared to the pituitary gland, pituitary tumors show higher expression levels of this gene.

Induction:Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B/interleukin-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. Repressed by HIPK2 and LIMD1

Isoforms & Post-Translational Modification：Q16665 has 3 isomers: Q16665-1: 92670 Da (predicted); Q16665-2: 82746 Da (predicted); Q16665-3: 95634 Da (predicted).
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 (PubMed:20699359, PubMed:20889502). Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome (By similarity);Sumoylated; with SUMO1 under hypoxia (PubMed:15465032, PubMed:15776016, PubMed:17610843). Sumoylation is enhanced through interaction with RWDD3 (PubMed:17956732). Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia (PubMed:15465032, PubMed:15776016, PubMed:17610843). 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 (PubMed:15465032, PubMed:15776016, PubMed:17610843). Desumoylation by SENP1 increases its stability amd transcriptional activity (By similarity). There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity (Probable);Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation (PubMed:12464182). Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (PubMed:24681946);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 E3 ligase VHL (PubMed:25615526). Deubiquitinated by UCHL1 (PubMed:25615526);In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). EGLN3/PHD3 has also been shown to hydroxylate Pro-564 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Deubiquitinated by USP20 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation (PubMed:12080085). This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol (PubMed:12080085). Repressed by iron ion, via Fe(2+) prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation (PubMed:28296633);The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains;(Microbial infection) Glycosylated at Arg-18 by enteropathogenic E.coli protein NleB1: arginine GlcNAcylation enhances transcription factor activity and impairs glucose metabolism

Subunit：Interacts with the ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:10944113, PubMed:20699359). Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability (By similarity). Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2 (PubMed:11959990, PubMed:12778114, PubMed:16543236, PubMed:16973622, PubMed:8917528, PubMed:9887100). Interacts with CREBBP (via TAZ-type 1 domains) (PubMed:11959977, PubMed:8917528). Interacts with NCOA1, NCOA2, APEX1 and HSP90 (PubMed:10202154, PubMed:10594042). Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation (PubMed:14757845). During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A (PubMed:10944113, PubMed:11006129, PubMed:12004076, PubMed:12050673, PubMed:16862177). Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription (By similarity). Interacts (via the ODD domain) with NAA10; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia (PubMed:12464182, PubMed:16288748). Interacts with RWDD3; the interaction enhances HIF1A sumoylation (PubMed:17956732, PubMed:23469069). Interacts with TSGA10 (By similarity). Interacts with HIF3A (By similarity). Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability (PubMed:18658046). Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia-mimicking conditions (PubMed:11389899). Interacts with USP20 (PubMed:15776016). Interacts with RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation (PubMed:17244529). Interacts (via N-terminus) with USP19 (PubMed:22128162). Interacts with SIRT2 (PubMed:24681946). Interacts (deacetylated form) with EGLN1 (PubMed:24681946). Interacts with CBFA2T3 (PubMed:25974097). Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842). Interacts with DCUN1D1; this interaction increases the interaction between VHL and DCUN1D1 (PubMed:23401859). Interacts with HIF1AN (PubMed:12446723)

Synonyms

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

Documentation

User Guide for Antibodies (1077 KB)