PHD3 (EGLN3) (NM_022073) Human Recombinant Protein

CAT#: TP310319

Recombinant protein of human egl nine homolog 3 (C. elegans) (EGLN3)


  View other "EGLN3" proteins (3)

USD 823.00

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Size
    • 20 ug

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Specifications

Product Data
Species Human
Expression Host HEK293T
Expression cDNA Clone or AA Sequence
>RC210319 protein sequence
Red=Cloning site Green=Tags(s)

MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQLAGPRAGVSK
RHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPN
GDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTV
WYFDAEERAEAKKKFRNLTRKTESALTED

TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag C-Myc/DDK
Predicted MW 27.1 kDa
Concentration >50 ug/mL as determined by microplate BCA method
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol
Preparation Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
Note For 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
Cytogenetics 14q13.1
Refseq Size 2722
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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