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AB82884

Anti-PHD1/prolyl hydroxylase antibody [PHD112/G7]

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(1 Publication)

Mouse Monoclonal PHD1/prolyl hydroxylase antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human EGLN2.

View Alternative Names

EIT6, EGLN2, 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

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

PHD112/G7

Isotype

IgM

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human EGLN2.

Q96KS0

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
Preservative: 0.02% Sodium azide Constituents: 99.98% PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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.
Biological function summary

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.

Pathways

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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).
See full target information EGLN2

Publications (1)

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PloS one 6:e23847 PubMed21887331

2011

Overexpression of the HIF hydroxylases PHD1, PHD2, PHD3 and FIH are individually and collectively unfavorable prognosticators for NSCLC survival.

Applications

IHC-P

Species

Human

Sigve Andersen,Tom Donnem,Helge Stenvold,Samer Al-Saad,Khalid Al-Shibli,Lill-Tove Busund,Roy M Bremnes
View all publications

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