HIF-1α (Acetyl Lys532) rabbit pAb
Produktgrößen
50UL
£ POA
ES20097-50UL
100UL
£ POA
ES20097-100UL
Über dieses Produkt
- SKU:
- ES20097
- Zusätzliche Namen:
- 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)
- Anwendung:
- Western Blot, ELISA
- Klonalität:
- Polyclonal
- Konzentration:
- 1 mg/ml
- Weitere Details:
- 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.;
- Immunogen:
- Synthesized peptide derived from human HIF-1α (Acetyl Lys532)
- Isotyp:
- IgG
- Reaktivitäten:
- Human, Mouse, Rat
- Versandbedingungen:
- Blue Ice
- Quelle:
- Rabbit
- Lagerbedingungen:
- -20[o]C
- Hersteller:
- ELK Biotechnology
- Typ:
- Antibodies: Polyclonal Antibody