Anti-FIH [FIH162C]
Invented by Helen Turley from University of Oxford
Invented at University of Oxford
- Datasheet
- References (10)
- Inventor Info
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: 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
Add a reference
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
