PHD3 (EGLN3) (NM_022073) Human Recombinant Protein

Specifications

Product Data
Species	Human
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >RC210319 protein sequence Red=Cloning site Green=Tags(s) MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQLAGPRAGVSK RHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPN GDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTV WYFDAEERAEAKKKFRNLTRKTESALTED TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-Myc/DDK
Predicted MW	27.1 kDa
Concentration	>0.05 µg/µL as determined by microplate BCA method
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Preparation	Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
Note	For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage	Store at -80°C.
Stability	Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Reference Data
RefSeq	NP_071356
Locus ID	112399
UniProt ID	Q9H6Z9
Refseq Size	2722
Cytogenetics	14q13.1
Refseq ORF	717
Synonyms	HIFP4H3; HIFPH3; PHD3
Summary	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. EGLN3 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. Target proteins are preferentially recognized via a LXXLAP motif.[UniProtKB/Swiss-Prot Function]
Protein Families	Druggable Genome
Protein Pathways	Pathways in cancer, Renal cell carcinoma

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