Recombinant Human EGLN3 Protein, Myc/DDK-tagged, C13 and N15-labeled
Cat.No. : | EGLN3-2544H |
Product Overview : | EGLN3 MS Standard C13 and N15-labeled recombinant protein (NP_071356) with a C-terminal MYC/DDK tag, was expressed in HEK293 cells. |
- Specification
- Gene Information
- Related Products
Description : | 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 (Probable). |
Source : | HEK293 |
Species : | Human |
Tag : | Myc/DDK |
Molecular Mass : | 27.3 kDa |
AA Sequence : | MPLGHIMRLDLEKIALEYIVPCLHE VGFCYLDNFLGEVVGDCVLERVKQL HCTGALRDGQLAGPRAGVSKRHLRG DQITWIGGNEEGCEAISFLLSLIDR LVLYCGSRLGKYYVKERSKAMVACY PGNGTGYVRHVDNPNGDGRCITCIY YLNKNWDAKLHGGILRIFPEGKSFI ADVEPIFDRLLFFWSDRRNPHEVQP SYATRYAMTVWYFDAEERAEAKKKF RNLTRKTESALTEDTRTRPLEQKLI SEEDLAANDILDYKDDDDKV |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : | Stable for 3 months from receipt of products under proper storage and handling conditions. |
Storage : | Store at -80 centigrade. Avoid repeated freeze-thaw cycles. |
Concentration : | 50 μg/mL as determined by BCA |
Storage Buffer : | 100 mM glycine, 25 mM Tris-HCl, pH 7.3. |
Gene Name : | EGLN3 egl-9 family hypoxia inducible factor 3 [ Homo sapiens (human) ] |
Official Symbol : | EGLN3 |
Synonyms : | EGLN3; egl nine homolog 3 (C. elegans); EGL nine (C.elegans) homolog 3; egl nine homolog 3; HIF prolyl hydroxylase 3; HIFPH3; PHD3; HPH-1; HPH-3; HIF-PH3; HIF-prolyl hydroxylase 3; egl nine-like protein 3 isoform; hypoxia-inducible factor prolyl hydroxylase 3; prolyl hydroxylase domain-containing protein 3; FLJ21620; MGC125998; MGC125999; |
Gene ID : | 112399 |
mRNA Refseq : | NM_022073 |
Protein Refseq : | NP_071356 |
MIM : | 606426 |
UniProt ID : | Q9H6Z9 |
Products Types
◆ Recombinant Protein | ||
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EGLN3-400H | Recombinant Human EGLN3 Protein, MYC/DDK-tagged | +Inquiry |
EGLN3-1688R | Recombinant Rat EGLN3 Protein, His (Fc)-Avi-tagged | +Inquiry |
EGLN3-2681M | Recombinant Mouse EGLN3 Protein, His (Fc)-Avi-tagged | +Inquiry |
◆ Lysates | ||
EGLN3-6693HCL | Recombinant Human EGLN3 293 Cell Lysate | +Inquiry |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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