ELISA/assay

Human hypoxia-inducible factor 1alpha (HIF-1alpha) ELISA Kit

MBS703254

48-Strip-Wells

565 USD

ELISA Kit

Human hypoxia-inducible factor 1alpha (HIF-1alpha) ELISA Kit

hypoxia-inducible factor 1alpha (HIF-1alpha)

hypoxia-inducible factor 1alpha (HIF-1alpha); hypoxia-inducible factor 1a (HIF-1a) ; HIF-1alpha; HIF1; HIF1-ALPHA; MOP1; PASD8; bHLHe78; ARNT interacting protein hypoxia-inducible factor 1 alpha isoform I.3 hypoxia-inducible factor 1; alpha subunit hypoxi

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

HIF-1alpha

HIF-1a

HIF1A; HIF1A; HIF1; MOP1; PASD8; bHLHe78; HIF-1alpha; HIF1-ALPHA; BHLHE78; MOP1; PASD8

HIF1A_HUMAN

Human

This assay has high sensitivity and excellent specificity for detection of human HIF-1alpha. No significant cross-reactivity or interference between human HIF-1alpha and analogues was observed.

Unopened test kits should be stored at 2 to 8 degree C upon receipt. Please refer to pdf manual for further storage instructions.

Samples: Serum, plasma, tissue homogenates. Assay Type: Sandwich. Detection Range: 62.5 pg/ml -4000 pg/ml. Sensitivity: 15.6 pg/ml.

Intra-assay Precision: Intra-assay Precision (Precision within an assay): CV%<8%. Three samples of known concentration were tested twenty times on one plate to assess. Inter-assay Precision: Inter-assay Precision (Precision between assays): CV%<10%. Three samples of known concentration were tested in twenty assays to assess.

Principle of the Assay This assay employs the quantitative sandwich enzyme immunoassay technique. Antibody specific for HIF-1alpha has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any HIF-1alpha present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for HIF-1alpha is added to the wells. After washing, avidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of HIF-1alpha bound in the initial step. The color development is stopped and the intensity of the color is measured.

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.

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810

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2750

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