HIF1A | HIF1-alpha Rabbit pAb, BF488 conj. (标记一抗) | Bioss

bs-0737R-BF488

HIF1A | HIF1-alpha Rabbit pAb, BF488 conj.

BF488标记的缺氧诱导因子1α /低氧诱导因子-1抗体

ARNT interacting protein; ARNT-interacting protein; Basic helix loop helix PAS protein MOP1; Basic-helix-loop-helix-PAS protein MOP1; bHLHe78; Class E basic helix-loop-helix protein 78; HIF 1A; HIF 1alpha; HIF-1-alpha; HIF1 A; HIF1 alpha; HIF1; HIF1-alpha; HIF1A; HIF1A_HUMAN; Hypoxia inducible factor 1 alpha; Hypoxia inducible factor 1 alpha isoform I.3; Hypoxia inducible factor 1 alpha subunit; Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor; Hypoxia inducible factor 1, alpha subunit(basic helix loop helix transcription factor); Hypoxia inducible factor1alpha; Hypoxia-inducible factor 1-alpha; Hypoxia-inducible factor-1a; Member of PAS protein 1; Member of PAS superfamily 1; Member of the PAS Superfamily 1; MOP 1; MOP1; PAS domain-containing protein 8; PASD 8; PASD8.

BF488
Excitation spectrum: 488nm
Emission spectrum: 519nm

Rabbit

KLH conjugated synthetic peptide derived from middle of human HIF-1 Alpha: 341-450/826

IgG

affinity purified by Protein A

Polyclonal

92 kDa

1mg/ml

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

缺氧诱导因子1α不仅对于机体在缺氧条件下维持正常的生理功能具有特别重要的意义,并在肿瘤的生长以及神经细胞凋亡等病理过程中起重要作用. HIF1 alpha能调节许多下游基因的表达水平.
哺乳动物细胞在低氧压力条件下出现HIF。HIF是一种转录因子，对细胞的缺氧起稳定作用。

    缺氧诱导因子1Alpha不仅对于机体在缺氧条件下维持正常的生理功能具有特别重要的意义,并在肿瘤的生长以及神经细胞凋亡等病理过程中起重要作用. HIF1 alpha能调节许多下游基因的表达水平.
    哺乳动物细胞在低氧压力条件下出现HIF。HIF是一种转录因子，对细胞的缺氧起稳定作用。

HIF1A

Hypoxia-inducible factor 1-alpha

Interacts with COPS5 subunit of COP9 signalosome complex,leading to the regulation of its stability. Interacts with TSGA10(By similarity). Efficient DNA binding requires heterodimerizationof an alpha and a beta/ARNT subunit. Binds to the TAZ-type 1domains of CREBBP and EP300. Interacts with NCOA1, NCOA2, APEX andHSP90. Interacts with VHL which docks HFA1 to the E3 ubiquitinligase complex for subsequent destruction. Interaction, via the ODDdomain, with the beta domain of VHLL, protects HIF1A fromdestruction by competing against the destructive targetinginitiated by VHL.

Cytoplasm. Nucleus.

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.

In normoxia, is hydroxylated on Pro-402 and Pro-564 in theoxygen-dependent degradation domain (ODD) by EGLN1/PHD1 andEGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564.The hydroxylated prolines promote interaction with VHL, initiatingrapid ubiquitination and subsequent proteasomal degradation. Underhypoxia, proline hydroxylation is impaired and ubiquitination isattenuated, resulting in stabilization.
In normoxia, is hydroxylated on Asn-803 by HIF1AN, thusabrogating interaction with CREBBP and EP300 and preventingtranscriptional activation.
S-nitrosylation of Cys-800 may be responsible for increasedrecruitment of p300 coactivator necessary for transcriptionalactivity of HIF-1 complex.
Acetylation of Lys-532 by ARD1 increases interaction with VHLand stimulates subsequent proteasomal degradation.
Requires phosphorylation for DNA-binding.

Contains 1 basic helix-loop-helix (bHLH) domain.
Contains 1 PAC (PAS-associated C-terminal) domain.
Contains 2 PAS (PER-ARNT-SIM) domains.

Functions as a master transcriptional regulator of theadaptive response to hypoxia. Under hypoxic conditions activatesthe transcription of over 40 genes, including, erythropoietin,glucose transporters, glycolytic enzymes, vascular endothelialgrowth factor, and other genes whose protein products increaseoxygen delivery or facilitate metabolic adaptation to hypoxia.Plays an essential role in embryonic vascularization, tumorangiogenesis and pathophysiology of ischemic disease. Binds to coreDNA sequence 5'-[AG]CGTG-3' within the hypoxia response element(HRE) of target gene promoters. Activation requires recruitment oftranscriptional coactivators such as CREBPB and EP300. Activity isenhanced by interaction with both, NCOA1 or NCOA2. Interaction withredox regulatory protein APEX seems to activate CTAD andpotentiates activation by NCOA1 and CREBBP.