|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||43650 Da|
|Other Names||Egl nine homolog 2, Estrogen-induced tag 6, HPH-3, Hypoxia-inducible factor prolyl hydroxylase 1, HIF-PH1, HIF-prolyl hydroxylase 1, HPH-1, Prolyl hydroxylase domain-containing protein 1, PHD1, EGLN2, EIT6|
|Target/Specificity||A synthetic peptide corresponding to residues in human PHD1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PHD1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferentially recognized via a LXXLAP motif.|
|Tissue Location||Expressed in adult and fetal heart, brain, liver, lung, skeletal muscle, and kidney. Also expressed in testis and placenta. Highest levels in adult brain, placenta, lung, kidney, and testis. Expressed in hormone responsive tissues, including normal and cancerous mammary, ovarian and prostate epithelium.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Prolyl hydroxylase domain-containing protein 1 (PHD1, Hypoxia-inducible factor prolyl hydroxylase 1) is a 2-oxoglutarate and dioxygen-dependent enzyme that mediates the rapid destruction of hypoxia-inducible factor (HIF) alpha subunits (1) by catalyzing their post-translational formation. PHD1 functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. It is also suggested to play a role in cell growth regulation (2). Loss of PHD1 has been shown to lower oxygen consumption in skeletal muscle by reprogramming glucose metabolism from oxidative to more anaerobic ATP production through activation of a Pparalpha pathway (3). Studies in a wide variety of cell lines revealed a predominant species at the predicted molecular mass (44 kDa) and an additional species running at a slightly increased mobility (40 kDa) (4).
1. Barth S, et al. J Biol Chem. 284(34):23046-58, 2009 2. The UniProt Consortium. The Universal Protein Resource (UniProt), Nucleic Acids Res. 36:D190-D195 (2008) 3. Aragon閟 J, et al. Nat Genet. 40(2):170-80, 2008 4. Tian Ya-Min, et al. Biochem, J. 397:179 -186, 2006
If you have used an Abgent product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at firstname.lastname@example.org.