Anti-FIH [FIH162C]

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.

Contributors

Inventor Institute
Helen Turley University of Oxford
SKU: 151316
Product 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.
Conjugation: Unconjugated
Isotype: IgG1
Molecular weight: 40 kDa
Immunogen: Full length human FIH expressed in Escherichia coli BL21(DE3) cells.
Myeloma used: P3/NS1/1-Ag4.1
Cat. #: 151316
Tool sub type: Primary antibody
Unit size: 100 ug
Application: IHC ; IF ; WB
Target: Factor Inhibiting HIF1 (FIH)
Reactivity: Human
Clone: FIH162C
Host: Mouse
Class: Monoclonal
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.
Format: Liquid
Concentration: 1 mg/ml
Storage buffer: PBS with 0.02% azide
Storage conditions: -15° C to -25° C
Shipping conditions: Dry ice
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].

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