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Anti-FIH [FIH162C]

Invented by Helen Turley from University of Oxford
Invented at University of Oxford

Info

Catalogue Number 151316
Applications IHC IF WB
Antigen/Gene or Protein Targets Factor Inhibiting HIF1 (FIH)
Reactivity Human
Relevance 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.
Host Mouse
Immunogen Full length human FIH expressed in Escherichia coli BL21(DE3) cells.
Positive Control MCF7 cells
Subclass IgG1
Molecular Weight (kDa) 40
Myeloma Used P3/NS1/1-Ag4.1
Recommended Growing Conditions RPMI + 10% FCS + 5% CO2
Strain Balb/c
Research Area Cancer, Epigenetics & Nuclear Signalling

References

There are 10 reference entries for this reagent.

View All References

References: 10 entries

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.

Europe PMC ID: 22075993

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.

Europe PMC ID: 19724277

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).

Europe PMC ID: 17003112

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.

Europe PMC ID: 16324198

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].

Europe PMC ID: 15302861


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References: 10 entries

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].


Add a reference