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AB128449

Recombinant Human PHD3 protein (His tag N-Terminus)

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Recombinant Human PHD3 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 239 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Prolyl hydroxylase EGLN3, Egl nine homolog 3, HPH-1, Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, HIF-prolyl hydroxylase 3, HPH-3, PHD3, EGLN3

1 Images
SDS-PAGE - Recombinant Human PHD3 protein (His tag N-Terminus) (AB128449)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human PHD3 protein (His tag N-Terminus) (AB128449)

3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q9H6Z9

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.32% Tris HCl, 0.08% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.06% EDTA

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED","proteinLength":"Full Length","predictedMolecularWeight":"29.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":239,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9H6Z9","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

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
False
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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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Specifications

Form

Liquid

Additional notes

ab128449 is purified using conventional chromatography techniques (anion exchange and gel filtration)

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General info

Function

Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed : 19584355, PubMed : 20978507, PubMed : 21483450, PubMed : 21575608, PubMed : 21620138, PubMed : 22797300). Target proteins are preferentially recognized via a LXXLAP motif. 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 : 12181324). 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 : 12181324). Also hydroxylates HIF2A (PubMed : 11595184, PubMed : 12181324). Has a preference for the CODD site for both HIF1A and HIF2A (PubMed : 11595184, PubMed : 12181324). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (PubMed : 11595184, PubMed : 12181324). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed : 11595184, PubMed : 12181324). 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 : 12181324). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis (PubMed : 21483450, PubMed : 21620138). Under normoxia, hydroxylates and regulates the stability of ADRB2 (PubMed : 19584355). Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (PubMed : 20849813). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (PubMed : 16098468). Also essential for hypoxic regulation of neutrophilic inflammation (PubMed : 21317538). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (PubMed : 22797300). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable).

Post-translational modifications

Ubiquitinated by SIAH1 and/or SIAH2 in response to the unfolded protein response (UPR), leading to its degradation.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed : 19584355, PubMed : 20978507, PubMed : 21483450, PubMed : 21575608, PubMed : 21620138, PubMed : 22797300). Target proteins are preferentially recognized via a LXXLAP motif. 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 : 12181324). 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 : 12181324). Also hydroxylates HIF2A (PubMed : 11595184, PubMed : 12181324). Has a preference for the CODD site for both HIF1A and HIF2A (PubMed : 11595184, PubMed : 12181324). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (PubMed : 11595184, PubMed : 12181324). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed : 11595184, PubMed : 12181324). 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 : 12181324). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis (PubMed : 21483450, PubMed : 21620138). Under normoxia, hydroxylates and regulates the stability of ADRB2 (PubMed : 19584355). Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (PubMed : 20849813). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (PubMed : 16098468). Also essential for hypoxic regulation of neutrophilic inflammation (PubMed : 21317538). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (PubMed : 22797300). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable).
See full target information EGLN3
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