Cell Signaling Technology

Product Pathways - Translational Control

PHD-2/Egln1 (D31E11) Rabbit mAb #4835

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk Endogenous 50 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

PHD-2/Egln1 (D31E11) Rabbit mAb detects endogenous levels of total PHD-2/Egln1 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val226 of human PHD-2/Egln1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using PHD-2/Egln1 (D31F11) Rabbit mAb.

Background

PHD1 (Egln2), PHD-2 (Egln1), and PHD3 (Egln3) are members of the Egln family of proline hydroxylases. They function as oxygen sensors that catalyze the hydroxylation of HIF on prolines 564 and 402, initiating the first step of HIF degradation through the VHL/ubiquitin pathway (1,2). PHD1 is highly expressed in a wide array of tissues whereas PHD2 and PHD3 are expressed mainly in heart and skeletal muscle (1,3). The mRNA levels of PHD are upregulated by HIF through the hypoxia-response element under low oxygen conditions (4-7). These three enzymes also exhibit different peptide specificity target proteins, PHD1 and PHD2 can hydroxylate both proline 402 and proline 564, but PHD3 can only hydroxylate proline 564 (2,8). In addition to HIF, PHD enzymes have also has been shown to catalyze the hydroxylation of RNA polymerase subunits and myogenin (3,9).

  1. Freeman, R.S. et al. (2003) Mol Cells 16, 1-12.
  2. Villar, D. et al. (2007) Biochem J 408, 231-40.
  3. Fu, J. et al. (2007) J Biol Chem 282, 12410-8.
  4. D'Angelo, G. et al. (2003) J Biol Chem 278, 38183-7.
  5. del Peso, L. et al. (2003) J Biol Chem 278, 48690-5.
  6. Pescador, N. et al. (2005) Biochem J 390, 189-97.
  7. Metzen, E. et al. (2005) Biochem J 387, 711-7.
  8. Hirsilä, M. et al. (2003) J Biol Chem 278, 30772-80.
  9. Mikhaylova, O. et al. (2008) Mol Cell Biol 28, 2701-17.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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