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Contributor Information

  • Name Helen Turley
  • Institute University of Oxford

Tool Details

  • Tool name: Anti-FIH [FIH162C]
  • Clone: FIH162C
  • Tool type: Antibodies
  • Tool sub-type: Primary antibody
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Molecular weight of the target: 40 kDa
  • Application: IHC ; IF ; WB
  • Strain: Balb/c
  • Description: FIH, Factor Inhibiting HIF1 (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.
  • Immunogen: Full length human FIH expressed in Escherichia coli BL21(DE3) cells.
  • Isotype: IgG1
  • Research area: Cancer; Genetics
  • Myeloma used: P3/NS1/1-Ag4.1

  • For Research Use Only

Target Details

  • Target: Factor Inhibiting HIF1 (FIH)
  • Target molecular weight: 40 kDa
  • Target background: FIH, Factor Inhibiting HIF1 (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.

Application Details

  • Application: IHC ; IF ; WB

Handling

  • Format: Liquid
  • Concentration: 1 mg/ml
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15°C to -25°C
  • Shipping conditions: Shipping at 4°C

Documentation

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References

  • •  Wollenick et al. 2012. Nucleic Acids Res. 40(5):1928-43. PMID: 22075993.
  • •  Synthetic transactivation screening reveals ETV4 as broad coactivator of hypoxia-inducible factor signaling.
  • •  Yan et al. 2009. Br J Cancer. 101(7):1168-74. PMID: 19724277.
  • •  BRCA1 tumours correlate with a HIF-1alpha phenotype and have a poor prognosis through modulation of hydroxylase enzyme profile expression.
  • •  Cockman et al. 2006. Proc Natl Acad Sci U S A. 103(40):14767-72. PMID: 17003112.
  • •  Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
  • •  Soilleux et al. 2005. Histopathology. 47(6):602-10. PMID: 16324198.
  • •  Use of novel monoclonal antibodies to determine the expression and distribution of the hypoxia regulatory factors PHD-1, PHD-2, PHD-3 and FIH in normal and neoplastic human tissues.
  • •  Stolze et al. 2004. J Biol Chem. 279(41):42719-25. PMID: 15302861.
  • •  Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].