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BRAND / VENDOR: Abcam

Abcam, ab184714, Anti-PHD3 antibody [EPR17869]

CATALOG NUMBER: ab184714
Regular price$0.99
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal PHD3 antibody. Suitable for IP, WB, ICC/IF and reacts with Mouse, Rat, Human samples. Cited in 11 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR17869,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:WB, IP, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

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

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% 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

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The PHD3 protein also known as EGLN3 or Prolyl Hydroxylase Domain-Containing Protein 3 functions mechanically to regulate oxygen homeostasis in cells. It catalyzes the hydroxylation of proline residues on hypoxia-inducible transcription factors (HIFs). The molecular mass of PHD3 is approximately 27 kDa. PHD3 expresses in a variety of tissues notably in the heart brain and skeletal muscles. Its expression often occurs in response to hypoxic conditions reflecting its role in oxygen sensing and adaptation to change in oxygen levels.
Biological function summary
The PHD3 protein plays an essential role in regulating the degradation of HIFs preventing their accumulation under normoxic conditions. It is part of a larger complex which includes oxygen iron and 2-oxoglutarate facilitating its hydroxylase activity. Hydroxylation of HIFs by PHD3 marks them for degradation via the ubiquitin-proteasome pathway preventing HIFs from activating genes related to erythropoiesis angiogenesis and cellular metabolism adaptation to hypoxia. Through these actions PHD3 helps maintain cellular oxygen homeostasis and metabolic balance.
Pathways
PHD3 is integral to the HIF signaling pathway and the cellular response to hypoxia. Its interaction with HIF-1α and HIF-2α is important in this context dictating the stability and activity of these transcription factors under varying oxygen levels. PHD3 also associates with other prolyl hydroxylases such as PHD1 and PHD2 coordinating the regulation of HIFs collectively across different cell types and conditions. These interactions contribute to the modulation of gene expression in response to hypoxic stress.
Aberrant PHD3 activity links to cancer and ischemic diseases. In cancer altered PHD3 expression affects tumor growth and metastasis by disrupting normal oxygen sensing allowing cancer cells to adapt to low-oxygen environments. Moreover PHD3's interaction with proteins like HIF-1α and HIF-2α plays a role in the pathological angiogenesis seen in certain cancer types. In ischemic diseases improper regulation by PHD3 might impede normal tissue responses to reduced blood flow affecting recovery. Its specific modulation in diseases presents potential therapeutic targets for drug development.


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Collaboration

Tony Tang

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