Recombinant Mouse Egl nine homolog 3 protein (Egln3)

Code CSB-RP147974m
MSDS
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Egln3
Uniprot No.
Research Area
Others
Alternative Names
Egln3Egl nine homolog 3; EC 1.14.11.29; Hypoxia-inducible factor prolyl hydroxylase 3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; Prolyl hydroxylase domain-containing protein 3; PHD3; SM-20
Species
Mus musculus (Mouse)
Source
E.coli
Expression Region
2-239aa
Target Protein Sequence
PLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
31.2kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A. 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. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. 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. ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. 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. Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4.
Gene References into Functions
  1. we identified the beta2 adrenergic receptor (ADRB2) as a downstream target for PHD3 in skeletal muscle PMID: 28939592
  2. PHD3 could protect against cardiac perivascular fibrosis and improve myocardial function in an obstructive sleep apnea mouse model by inhibiting endothelial-to-mesenchymal transition. PMID: 29051216
  3. PHD3 expression induced by cytokines is NF-kappaB dependent in mesangial cells. Endogenously produced NO further augments PHD3 expression via HIF-1 alpha. PMID: 28054119
  4. Opposing regulation and roles for PHD3 in lung dendritic cells and alveolar macrophages PMID: 28716863
  5. Our observations disclose a novel role of PHD3 in the development of Tregs. PMID: 27331863
  6. PHD3 is an active participant in atherogenesis PMID: 26995088
  7. Cardiomyocyte-specific transgenic expression of PHD3 impairs the myocardial response to ischemia. PMID: 26044310
  8. PHD3 protects intestinal epithelial barrier function and reveal a hydroxylase-independent function of PHD3 in stabilizing occludin PMID: 26124271
  9. depletion of PHD3 leads to increased stabilization of HIF-1alpha and inhibition of DNA damage response, both of which may contribute to the cardioprotective effect seen with depletion of PHD3. PMID: 25633836
  10. PHD3 loss sustains cell proliferation through the control of EGFR. PMID: 25420773
  11. Using conditional PHD3-knockout mice, it was shown that PHD3 affects the production of Angptl2 and additionally influences the response toward this apoptosis-modulating factor. PMID: 24626957
  12. ablation of the PHD3 gene resulted in increased angiogenesis and cardiac function after infarction thereby offering a potential target for management of ischemic myocardial disease PMID: 23978105
  13. isoform-specific inhibition of Phd3 could be exploited to treat type 2 diabetes without the toxicity that could occur with chronic inhibition of multiple Phd isoforms. PMID: 24037093
  14. Egln3 suppresses glioma progression PMID: 22905089
  15. mice lacking PHD3 were resistant to the effects of ionizing radiation and had decreased thymic apoptosis, a biomarker of genomic integrity PMID: 22797300
  16. It is concluded that impairment of PHD3 enzyme function aggravates the clinical course of abdominal sepsis PMID: 22786772
  17. PHD3 has a role in regulating neutrophil survival in hypoxia PMID: 21317538
  18. EGLN3 has a role in the regulation of NF-kappaB and suggests that it is involved in mediating myogenic differentiation, which is HIF-independent PMID: 20089853
  19. PHD3 appears to be a tumor suppressor in colorectal cancer cells that inhibits IKKbeta/NF-kappaB signaling, independent of its hydroxylase activity. PMID: 19786027
  20. Egln1/2/3 play dual roles in chondrocyted growth, acting as oxygen sensors and mediators of late stage events in the cell cycle. PMID: 17044072
  21. the role of PHD3 in sympathoadrenal development extends beyond simple control of cell survival and organ mass, with functional PHD3 being required for proper anatomical and physiological integrity of the system PMID: 18332118
  22. Phd3 loss exacerbates the HIF activation, hepatic steatosis, dilated cardiomyopathy, and premature mortality. PMID: 19720742

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Subcellular Location
Nucleus. Cytoplasm.
Tissue Specificity
Highly expressed in cardiac and smooth muscle. Also high expression in brain, skeletal muscle and kidney. Low levels in lung.
Database Links
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