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Contributor Information

  • Name Helen Turley
  • Institute University of Oxford

Tool Details

  • Tool name: Anti-PHD2 [366G/76/3]
  • Clone: 366G/76/3
  • Tool type: Antibodies
  • Tool sub-type: Primary antibody
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Molecular weight of the target: 46.1 kDa
  • Application: FACS ; IHC ; WB
  • Strain: Balb/c
  • Description: 366G/76/3 recognises human prolyl hydroxylase 2 (PHD2), a 46kDa enzyme expressed abundantly in all tissues with the highest expression in testis
  • Immunogen: Residues 1-24 of PHD2
  • Isotype: IgG1
  • Research area: Cancer; Tissue-specific biology; Genetics; Metabolism
  • Myeloma used: P3/NS1/1-Ag4.1

  • For Research Use Only

Target Details

  • Target: Prolyl Hydroxylase 2 (PHD2)
  • Target molecular weight: 46.1 kDa
  • Target background: 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.

Application Details

  • Application: FACS ; IHC ; WB

Handling

  • Format: Liquid
  • Concentration: 1 mg/ml
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15°C to -25°C
  • Shipping conditions: Shipping at 4°C

Documentation

References

  •   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.