Rabbit Recombinant Monoclonal PHD1/prolyl hydroxylase antibody - conjugated to Alexa Fluor® 750.
IgG
Rabbit
Alexa Fluor® 750
Ex: 749nm, Em: 775nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A (PubMed:11595184, PubMed:12039559, PubMed:15925519, PubMed:16509823, PubMed:17114296, PubMed:23932902). Target proteins are preferentially recognized via a LXXLAP motif (PubMed:11595184, PubMed:12039559, PubMed:15925519). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (PubMed:11595184, PubMed:12039559, PubMed:12181324, PubMed:15925519, PubMed:19339211). Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (PubMed:11595184, PubMed:12039559, PubMed:12181324, PubMed:15925519). Also hydroxylates HIF2A (PubMed:11595184, PubMed:12039559, PubMed:15925519). Has a preference for the CODD site for both HIF1A and HIF2A (PubMed:11595184, PubMed:12039559, PubMed:15925519). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed:11595184, PubMed:12039559, PubMed:15925519). 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 (PubMed:11595184, PubMed:12039559, PubMed:15925519). EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle (PubMed:11595184, PubMed:12039559, PubMed:15925519). Also regulates susceptibility to normoxic oxidative neuronal death (PubMed:11595184, PubMed:12039559, PubMed:15925519). 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 (PubMed:23932902). Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions (PubMed:17114296). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity).
Prolyl hydroxylase EGLN2, Egl nine homolog 2, Estrogen-induced tag 6, HPH-3, Hypoxia-inducible factor prolyl hydroxylase 1, Prolyl hydroxylase domain-containing protein 1, EIT-6, HIF-PH1, HIF-prolyl hydroxylase 1, HPH-1, PHD1, EIT6, EGLN2
Rabbit Recombinant Monoclonal PHD1/prolyl hydroxylase antibody - conjugated to Alexa Fluor® 750.
Prolyl hydroxylase EGLN2, Egl nine homolog 2, Estrogen-induced tag 6, HPH-3, Hypoxia-inducible factor prolyl hydroxylase 1, Prolyl hydroxylase domain-containing protein 1, EIT-6, HIF-PH1, HIF-prolyl hydroxylase 1, HPH-1, PHD1, EIT6, EGLN2
IgG
Rabbit
Alexa Fluor® 750
Ex: 749nm, Em: 775nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
EPR2746
Affinity purification Protein A
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle, Store in the dark
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
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This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
This supplementary information is collated from multiple sources and compiled automatically.
Prolyl hydroxylase 1 (PHD1) also known as EGLN2 is an enzyme that hydroxylates specific proline residues within target proteins. This process of prolyl hydroxylation is critical for regulating protein stability. PHD1 shares structural similarities with other members of the 2-oxoglutarate-dependent dioxygenase family and includes a conserved iron-binding motif essential for its enzymatic activity. PHD1 has a molecular mass of approximately 46 kDa and is expressed in a variety of tissues with notable presence in skeletal muscle heart and the liver.
PHD1 modulates the stability of the hypoxia-inducible factor (HIF) proteins which are key regulators of oxygen homeostasis in the cell. Under normoxic conditions PHD1 hydroxylates specific proline residues on HIF-alpha marking it for degradation via the ubiquitin-proteasome pathway. This enzyme does not function as part of a larger protein complex but it plays a pivotal role in determining the cellular response to oxygen levels. Additionally PHD1 expression affects the metabolic adaptation processes and energy expenditure in cells.
PHD1 plays a role in the cellular response to hypoxia and is integral to the HIF signaling pathway. It interacts directly with HIF-alpha subunits mediating their degradation under normal oxygen conditions to ensure HIF activity remains inhibited. Additionally PHD1 is indirectly involved in modulating the angiogenesis pathway as it influences the availability of HIF-related transcription factors which promote transcription of vascular endothelial growth factor (VEGF) under low oxygen conditions. The interplay between PHD1 PHD2 and PHD3 ensures a fine-tuned regulation of the HIF pathway based on oxygen availability.
PHD1 has links to cancer progression and ischemic conditions. The enzyme’s activity is often altered in response to the aberrant hypoxic signaling found within tumors impacting cellular proliferation and survival. In ischemic conditions reduced PHD1 activity leads to stabilization of HIF proteins and adaptation responses aimed at tissue survival. Mutations or dysregulation in PHD1 expression have been observed in metabolic syndromes suggesting potential therapeutic targets. Through its control over hypoxia-related proteins PHD1 also interacts with von Hippel-Lindau (VHL) protein which is part of the E3 ubiquitin ligase complex important for HIF-alpha degradation.
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