Recombinant Rabbit monoclonal primary
HIF-2 alpha Recombinant Rabbit Monoclonal Antibody [JB24-42] (ET7107-32)
SiHa, rat lung tissue, human breast cancer tissue, human placenta tissue, mouse colon tissue, HUVEC.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Basic helix loop helix PAS protein MOP2 antibody; Basic-helix-loop-helix-PAS protein MOP2 antibody; bHLHe73 antibody; Class E basic helix-loop-helix protein 73 antibody; ECYT4 antibody; Endothelial PAS domain containing protein 1 antibody; Endothelial pas domain protein 1 antibody; Endothelial PAS domain-containing protein 1 antibody; EPAS 1 antibody; EPAS-1 antibody; EPAS1 antibody; EPAS1_HUMAN antibody; HIF 1 alpha like factor antibody; HIF 2 alpha antibody; HIF-1-alpha-like factor antibody; HIF-2-alpha antibody; HIF2-alpha antibody; HIF2A antibody; HLF antibody; Hypoxia inducible factor 2 alpha antibody; Hypoxia inducible factor 2 alpha subunit antibody; Hypoxia-inducible factor 2-alpha antibody; Member of PAS protein 2 antibody; Member of pas superfamily 2 antibody; MOP 2 antibody; MOP2 antibody; PAS domain-containing protein 2 antibody; PASD2 antibody
Expressed in most tissues, with highest levels in placenta, lung and heart. Selectively expressed in endothelial cells.
In normoxia, is probably hydroxylated on Pro-405 and Pro-531 by EGLN1/PHD1, EGLN2/PHD2 and/or EGLN3/PHD3. 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 (By similarity).; In normoxia, is hydroxylated on Asn-847 by HIF1AN thus probably abrogating interaction with CREBBP and EP300 and preventing transcriptional activation.; Phosphorylated on multiple sites in the CTAD.; The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.
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.