Cancer Research Technology
Log in Register
Menu

Anti-PHD2 [366G/76/3]

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

Info

Catalogue Number 151314
Applications FACS IHC WB
Antigen/Gene or Protein Targets Prolyl Hydroxylase 2 (PHD2)
Reactivity Human
Relevance 366G/76/3 recognises human prolyl hydroxylase 2 (PHD2), a 46kDa enzyme expressed abundantly in all tissues with the highest expression in testis. Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex, consisting of an alpha and beta subunit, which plays a key role in coordinating the cellular response to hypoxia. During normal oxygen conditions, the alpha subunit of HIF-1 is rapidly degraded, however when hypoxia occurs this degradation is suppressed and HIF-1 activates the transcription of various genes important for survival and adaptation to hypoxia. Prolyl hydroxylase 2 catalyses the hydroxylation of specific prolyl residues within the HIF-1 alpha subunit, thereby targeting this subunit for degradation.
Host Mouse
Immunogen Residues 1-24 of PHD2
Positive Control MCF7 cells
Subclass IgG1
Molecular Weight (kDa) 46.1
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

Jubb et al. 2009. Br J Cancer. 101(10):1749-57. PMID: 19844231.

Expression of delta-like ligand 4 (Dll4) and markers of hypoxia in colon cancer.

Europe PMC ID: 19844231

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

Jubb et al. 2009. Br J Cancer. 101(10):1749-57. PMID: 19844231.

Expression of delta-like ligand 4 (Dll4) and markers of hypoxia in colon cancer.

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