抗体

Anti-FIH (Asparaginyl hydroxylase) Monoclonal Antibody

MBS190544

0.1毫克

370美元

单克隆

小鼠

nonconjugated

FIH162C

抗体

Anti-FIH (Asparaginyl hydroxylase) Monoclonal Antibody

HIF1甲

hypoxia-inducible factor 1-alpha isoform 1; Hypoxia-inducible factor 1-alpha; hypoxia-inducible factor 1-alpha; HIF-1-alpha; OTTHUMP00000179061; OTTHUMP00000179062; OTTHUMP00000179063; member of PAS protein 1; ARNT interacting protein; ARNT-interacting protein; member of PAS superfamily 1; PAS domain-containing protein 8; basic-helix-loop-helix-PAS protein MOP1; class E basic helix-loop-helix protein 78; hypoxia-inducible factor 1 alpha isoform I.3; hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor); hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor); 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

HIF1甲

缺氧诱导因子1A;缺氧诱导因子1A;HIF1;MOP1;PASD8;bHLHe78;HIF-1alpha;HIF1-甲;BHLHE78;MOP1;PASD8

HIF1A_HUMAN

单克隆

IgG1

FIH162C

小鼠

人类

HIF1甲。 这抗体识别人类FIH

100ug in PBS, pH 7.4; 50% glycerol, 0.09% sodium azide. Purified by Protein G affinity chromatography.

This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

Immunoblot

Immunoblotting: Use at 1-10ug/ml. A band of ~45kDa is detected. IHC/ICC: Use at 1-10ug/ml on frozen and paraffin-embedded samples. IFA: Use at 1-10ug/ml. See Stolze IP et al. 2004 J Biol Chem 279: 42719. These are recommended concentrations. User should determine optimal concentrations for their application.

Antigen: Recombinant full-length human FIH expressed in E. coli.

Dilution Instructions: Dilute in PBS or medium which is identical to that used in the assay system.

FIH, Factor Inhibiting HIF-1 (hypoxia-inducible factor), is an asparaginyl hydroxylase. FIH, in conjunction with VHL, represses HIF-1 transcriptional activity by disrupting the interaction of HIF-1 with the transcriptional coactivators CBP/p300, and by recruiting histone deacetylases. FIH activity is inhibited during hypoxia. Recent studies show that low nuclear expression of FIH is a prognostic indicator for poor overall survival in cases of clear cell renal cell carcinoma.

4504385

NP_001521.1

NM_001530.3

Q16665

92,670 Da

Adipogenesis Pathway 198832!!Angiogenesis Pathway 198772!!HIF-1-alpha Transcription Factor Network Pathway 138045!!Hypoxic And Oxygen Homeostasis Regulation Of HIF-1-alpha Pathway 138056!!Notch-mediated HES/HEY Network Pathway 169347!!PDGFR-beta Signaling Pathway 138071!!Pathways In Cancer 83105!!Renal Cell Carcinoma Pathway 83107!!Renal Cell Carcinoma Pathway 519!!Signaling Events Mediated By VEGFR1 And VEGFR2 Pathway 137940

This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes, including those involved in energy metabolism, angiogenesis, apoptosis, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq]

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. Ref.14 Ref.19 Ref.21 Ref.28 Ref.32 Ref.33 Ref.34. Subunit structure: 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 EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (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. By similarity. Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia-mimicking conditions. Interacts with USP20. Interacts with GNB2L1/RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation. Ref.9 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38. Subcellular location: Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia. Ref.11. 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. Induction: Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B/interleukin-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. 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). Ref.10 Ref.12 Ref.13. Post-translational modification: 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. Deubiquitinated by USP20. 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. This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol.S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.Requires phosphorylation for DNA-binding.Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity. By similarity. Ref.28 Ref.34 Ref.35Ubiquitinated; 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. Ref.12 Ref.18 Ref.19 Ref.21 Ref.30 Ref.33 Ref.37 Ref.39The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. Sequence similarities: Contains 1 basic helix-loop-helix (bHLH) domain.Contains 1 PAC (PAS-associated C-terminal) domain.Contains 2 PAS (PER-ARNT-SIM) domains.

0.1毫克

370美元