Ordering Information
- : ABE279
- : 100 μg
- : 1 mg/mL
Product Images
Western Blotting Analysis:
Representative lot data.
Cobalt chloride untreated and treated MCF-7 cell lysates were resolved by electrophore...
Anti-HIF-1α Antibody
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H | WB | Rabbit | Affinity Purified | Polyclonal Antibody |
Description:
Anti-HIF-1α Antibody | ABE279
Promotional Text:
Molecular Weight:
~100 kDa observed
Epitope:
0
Immunogen:
KLH-conjugated linear peptide corresponding to human HIF-1α.
Background Information:
Cell 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.
Species Reactivity:
Human
Species Reactivity Note:
Demonstrated to react with Human.
Control:
Cobalt chloride untreated and treated MCF-7 cell lysates
Quality Assurance:
Evaluated 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.
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.
Purification Method:
Affinity purified
Presentation:
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage Conditions:
Stable for 1 year at 2-8°C from date of receipt.
UniProt Number:
Entrez Gene Number:
Gene Symbol:
- HIF-1alpha
- HIF1
- HIF1-ALPHA
- MOP1
- PASD8
- bHLHe78
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
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.
Key Applications:
Western Blotting
Entrez Gene Summary:
Hypoxia-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].
UniProt Summary:
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.
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.
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.
Product Name:
Anti-HIF-1α
Concentration:
1 mg/mL
Antibody Type:
Polyclonal Antibody
Qty/Pk:
100 μg
Format:
Affinity Purified
Host:
Rabbit