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ABE279 Anti-HIF-1α Antibody

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ABE279
100 µg  
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Overview

Replacement Information

Key Specifications Table

Species ReactivityKey ApplicationsHostFormatAntibody Type
HWBRbAffinity PurifiedPolyclonal Antibody
Description
Catalogue NumberABE279
Replaces04-1006
DescriptionAnti-HIF-1α Antibody
Alternate Names
  • ARNT interacting protein
  • ARNT-interacting protein
  • Basic-helix-loop-helix-PAS protein MOP1
  • HIF-1 alpha
  • HIF1 alpha
  • Member of PAS protein 1
  • hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
  • hypoxia-inducible factor 1, alpha subunit
  • hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
  • member of PAS superfamily 1
Background InformationCell growth and viability is compromised by oxygen deprivation (hypoxia). Hypoxia-inducible factors, including HIF-1α, HIF-1β (also designated Arnt 1), EPAS-1 (also designated HIF-2α) and HIF-3α, induce glycolysis, erythropoiesis and angiogenesis in order to restore oxygen homeostasis. Hypoxia-inducible factors are members of the Per-Arnt-Sim (PAS) domain transcription factor family. In response to hypoxia, HIF-1α is upregulated and forms a heterodimer with Arnt 1 to form the HIF-1 complex. The HIF-1 complex recognizes and binds to the hypoxia responsive element (HRE) of hypoxia-inducible genes, thereby activating transcription. Hypoxia-inducible expression of some genes such as Glut-1, p53, p21 or Bcl-2, is HIF-1α dependent, whereas expression of others, such as p27, GADD 153 or HO-1, is HIF-1α independent. EPAS-1 and HIF-3α have also been shown to form heterodimeric complexes with Arnt 1 in response to hypoxia.
References
Product Information
FormatAffinity Purified
HS Code3002 15 90
Control
  • Cobalt chloride untreated and treated MCF-7 cell lysates
PresentationPurified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Quality LevelMQ100
Applications
ApplicationAnti-HIF-1α Antibody is a Rabbit Polyclonal Antibody for detection of HIF-1 alpha also known as ARNT interacting protein or HIF-1 alpha & has been validated in WB.
Key Applications
  • Western Blotting
Biological Information
ImmunogenKLH-conjugated linear peptide corresponding to human HIF-1α.
ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
HostRabbit
Species Reactivity
  • Human
Antibody TypePolyclonal Antibody
Entrez Gene Number
Entrez Gene SummaryHypoxia-inducible factor-1 (HIF1) is a transcription factor found in mammalian cells cultured under reduced oxygen tension that plays an essential role in cellular and systemic homeostatic responses to hypoxia. HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator (ARNT). This gene encodes the alpha subunit of HIF-1. Overexpression of a natural antisense transcript (aHIF) of this gene has been shown to be associated with nonpapillary renal carcinomas. Two alternative transcripts encoding different isoforms have been identified. [provided by RefSeq].
Gene Symbol
  • HIF-1alpha
  • HIF1
  • HIF1-ALPHA
  • MOP1
  • PASD8
  • bHLHe78
Purification MethodAffinity Purfied
UniProt Number
UniProt SummaryFUNCTION: 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.

SIZE: 826 amino acids; 92670 Da

SUBUNIT: Interacts with COPS5 subunit of COP9 signalosome complex, leading to the regulation of its stability. Interacts with TSGA10 (By similarity). Efficient DNA binding requires heterodimerization of an alpha and a beta/ARNT subunit. Binds to the TAZ-type 1 domains of CREBBP and EP300. Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts with VHL which docks HFA1 to the E3 ubiquitin ligase complex for subsequent destruction. Interaction, via the ODD domain, with the beta domain of VHLL, protects HIF1A from destruction by competing against the destructive targeting initiated by VHL.

SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in normoxia, nuclear translocation in response to hypoxia.

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.

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).

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. & In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. & S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex. & Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation. & Requires phosphorylation for DNA-binding.

SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain. & Contains 1 PAC (PAS-associated C-terminal) domain. & Contains 2 PAS (PER-ARNT-SIM) domains.
Molecular Weight ~100 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality AssuranceEvaluated by Western Blot in cobalt chloride untreated and treated MCF-7 cell lysates.

Western Blot Analysis: 1 µg/mL of this antibody detected HIF-1α on 10 µg of cobalt chloride untreated and treated MCF-7 cell lysates.
Usage Statement
  • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage ConditionsStable for 1 year at 2-8°C from date of receipt.
Packaging Information
Material Size100 µg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
ABE279 04053252483141

Documentation

Anti-HIF-1α Antibody SDS

Title

Safety Data Sheet (SDS) 

Anti-HIF-1α Antibody Certificates of Analysis

TitleLot Number
Anti-HIF-1 - 2051928 2051928
Anti-HIF-1 - 2199699 2199699
Anti-HIF-1 - 2278559 2278559
Anti-HIF-1 - 2366602 2366602
Anti-HIF-1 - NRG1854599 NRG1854599
Anti-HIF-1α - 3143167 3143167
Anti-HIF-1α - 3323026 3323026
Anti-HIF-1α - 4145810 4145810
Anti-HIF-1α -2520509 2520509
Anti-HIF-1α -2594416 2594416

References

Reference overviewPub Med ID
The organic solute transporters alpha and beta are induced by hypoxia in human hepatocytes.
Schaffner, CA; Mwinyi, J; Gai, Z; Thasler, WE; Eloranta, JJ; Kullak-Ublick, GA
Liver international : official journal of the International Association for the Study of the Liver  35  1152-61  2015

Show Abstract
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