EGLN3/PHD3 Antibody (EG188e/d5) [FITC] Summary
Immunogen |
Partial recombinant human PHD3/HIF Prolyl Hydroxylase 3 (UniProt# Q9H6Z9) |
Localization |
Cytoplasm. Nucleus. |
Predicted Species |
Mouse (98%), Bovine (98%), Primate (99%). Backed by our 100% Guarantee. |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
EGLN3 |
Purity |
Protein G purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunohistochemistry
- Immunohistochemistry-Paraffin
- Simple Western
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
PBS |
Preservative |
0.05% Sodium Azide |
Purity |
Protein G purified |
Notes
This conjugate is made on demand. Actual recovery may vary from the stated volume of this product. The volume will be greater than or equal to the unit size stated on the datasheet.
Alternate Names for EGLN3/PHD3 Antibody (EG188e/d5) [FITC]
Background
HIF prolyl 4-hydroxylases (PHDs) are proyl hydroxylase domain-containing enzymes (PHD1/ Egln2, PHD2/ Egln1, PHD3/ Egln3, and P4H-TM) which are known for their role in mediating physiological responses to hypoxic stress via modulation of HIF1alpha expression levels. HIF-alpha subunit is regulated by hydroxylation, both by a family of PHDs leading to ubiquitination and proteasomal degradation, and by transcriptional inactivation following asparaginyl hydroxylation by FIH (factor inhibiting HIF). When oxygen levels are normal, HIF Prolyl Hydroxylase 3 (HIF-PH3/ PHD3/ Egln3) hydroxylates a specific proline found in HIF1A'a NODD/CODD domains and also hydroxylates HIF2A with preference for CODD site for HIF1A/HIF2A. Once hydroxylated, HIFs undergo proteasomal degradation via von Hippel-Lindau (VHL) ubiquitination complex. Upon hypoxic trigger, the hydroxylation reaction is tempered which let HIFs to escape degradation process leading to their nuclear translocation, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. HIF-PH3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Besides HIFs, in hypoxic conditions HIF-PH3 also hydroxylates PKM (thereby limiting glycolysis) and hydroxylates/regulates the stability of ADRB2. In cardiomyocytes, HIF-PH3 inhibits Bcl2's anti-apoptotic effect by disrupting the BAX-BCL2 complex, and in neurons, HIF-PH3 has a NGF-induced proapoptotic effect mediated via CASP3 activity regulation. HIF-PH3 also plays a crucial role in DNA damage response by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Secondary Antibodies
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