Product Pathways - Translational Control
FIH (D19B3) Rabbit mAb #4426
|4426S||100 µl (10 western blots)||---||In Stock||---|
|4426||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||42||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
FIH (D19B3) Rabbit mAb detects endogenous levels of total FIH protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr35 of human FIH protein.
FIH (Factor inhibiting HIF-1, HIF asparagine hydroxylase) is a dioxygen-dependent asparaginyl hydroxylase that modifies target protein function by hydroxylating target protein asparagine residues (1-3). Hypoxia-inducible factor (HIF), a transcriptional activator involved in control of cell cycle in response to hypoxic conditions, is an important target for FIH regulation. FIH functions as an oxygen sensor that regulates HIF function by hydroxylating at Asn803 in the carboxy-terminal transactivation domain (CAD) of HIF (4,5). During normoxia, FIH uses cellular oxygen to hydroxylate HIF-1 and prevent interaction of HIF-1 with transcriptional coactivators, including the CBP/p300-interacting transactivator. Under hypoxic conditions, FIH remains inactive and does not inhibit HIF, allowing the activator to regulate transcription of genes in response to low oxygen conditions (4-6). FIH activity is regulated in through interaction with proteins, including Siah-1, which targets FIH for proteasomal degradation (7). The Cut-like homeodomain protein CDP can bind the FIH promoter region to regulate FIH expression at the transcriptional level (8). Phosphorylation of HIF at Thr796 also can prevent FIH hydroxylation on Asn803 (9). Potential FIH substrates also include proteins with ankyrin repeat domains, such as Iκ-B, Notch, and ASB4 (10-12).
- Koivunen, P. et al. (2004) J Biol Chem 279, 9899-904.
- Linke, S. et al. (2004) J Biol Chem 279, 14391-7.
- Lisy, K. and Peet, D.J. (2008) Cell Death Differ 15, 642-9.
- Mahon, P.C. et al. (2001) Genes Dev 15, 2675-86.
- Lando, D. et al. (2002) Genes Dev 16, 1466-71.
- Lando, D. et al. (2002) Science 295, 858-61.
- Fukuba, H. et al. (2007) Biochem Biophys Res Commun 353, 324-9.
- Li, J. et al. (2007) Mol Cell Biol 27, 7345-53.
- Lancaster, D.E. et al. (2004) Biochem J 383, 429-37.
- Ferguson, J.E. et al. (2007) Mol Cell Biol 27, 6407-19.
- Cockman, M.E. et al. (2006) Proc Natl Acad Sci USA 103, 14767-72.
- Cockman, M.E. et al. (2009) Mol Cell Proteomics 8, 535-46.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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