Cancer Research Technology
Log in Register
Menu

Anti-PHD3 [EG188e/d5]

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

Info

Catalogue Number 151315
Applications IHC WB
Antigen/Gene or Protein Targets Prolyl Hydroxylase 3 (PHD3)
Reactivity Human
Relevance PHD3 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins, hydroxylates HIF-1 alpha at Pro-564, and also hydroxylates HIF-2 alpha. It functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitylation complex. It may play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. It promotes cell death through a caspase-dependent mechanism
Host Mouse
Immunogen Residues 1-100 of human PHD3
Positive Control ZR75 cells on hypoxic induction
Subclass IgG1
Molecular Weight (kDa) 27.3
Myeloma Used P3/NS1/1-Ag4.1
Recommended Growing Conditions RPMI + 10% FCS + 5% CO2
Strain Balb/c
Research Area Cancer, Cardiovascular, Epigenetics & Nuclear Signalling, Metabolism

References

There are 8 reference entries for this reagent.

View All References

References: 8 entries

Fujita et al. 2012. J Biol Chem. 287(47):39942-53. PMID: 22948157.

Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-α (TNF-α) on cells of the nucleus pulposus through co-activation of nuclear factor κB (NF-κB)/p65 signaling.

Europe PMC ID: 22948157

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.

Appelhoff et al. 2004. J Biol Chem. 279(37):38458-65. PMID: 15247232.

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

Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor.

Europe PMC ID: 15247232


Add a reference

References: 8 entries

Fujita et al. 2012. J Biol Chem. 287(47):39942-53. PMID: 22948157.

Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-α (TNF-α) on cells of the nucleus pulposus through co-activation of nuclear factor κB (NF-κB)/p65 signaling.

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.

Appelhoff et al. 2004. J Biol Chem. 279(37):38458-65. PMID: 15247232.

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].

Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor.


Add a reference