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AB312080

Alexa Fluor® 555 Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

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Rabbit Recombinant Monoclonal PHD1/prolyl hydroxylase antibody - conjugated to Alexa Fluor® 555.

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

  • 578 PE

    PE Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • 660 APC

    APC Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • HRP

    HRP Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • 665 Alexa Fluor® 647

    Alexa Fluor® 647 Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • 617 Alexa Fluor® 594

    Alexa Fluor® 594 Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • 603 Alexa Fluor® 568

    Alexa Fluor® 568 Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • 775 Alexa Fluor® 750

    Alexa Fluor® 750 Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • Unconjugated

    Anti-PHD1/prolyl hydroxylase antibody [EPR2745]

  • Carrier free

    Anti-PHD1/prolyl hydroxylase antibody [EPR2745] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR2745

Isotype

IgG

Conjugation

Alexa Fluor® 555

Excitation/Emission

Ex: 555nm, Em: 565nm

Carrier free

No

Applications

Target Binding Affinity, Antibody Labelling

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

How are conjugated primary antibodies validated?
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.

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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|Store in the dark
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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.
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Product protocols

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