Recombinant Mouse Egl nine homolog 2 (Egln2)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

Egln2

Purity

>85% (SDS-PAGE)

Target Names

Egln2

Uniprot NO.

Q91YE2

Alternative Names

Egln2Egl nine homolog 2; EC 1.14.11.29; Falkor; Hypoxia-inducible factor prolyl hydroxylase 1; HIF-PH1; HIF-prolyl hydroxylase 1; HPH-1; Prolyl hydroxylase domain-containing protein 1; PHD1

Species

Mus musculus (Mouse)

Source

Yeast

Expression Region

1-419

Target Protein Sequence

MDSPCQPQAL NQALPQLPGS VSESLESSRA RMGVESYLPC PLLPAYHRPG ASGEASAGNG TPRTTATATT TTASPLREGF GGQDGGELWP LQSEGAAALV TKECQRLAAQ GARPEAPKRK WAKDGGDAPS PSKRPWARQE NQEAKGESGM GCDSGASNSS SSSSNTTSSS GEASARLREE VQPSAPERLA LDYIVPCMRY YGICVKDNFL GAVLGGRVLA EVEALKWGGR LRDGQLVSQR AIPPRSIRGD QIAWVEGHEP GCRSIGALMA HVDAVIRHCA GRLGNYVING RTKAMVACYP GNGLGYVRHV DNPHGDGRCI TCIYYLNQNW DVKVHGGLLQ IFPEGRPVVA NIEPLFDRLL IFWSDRRNPH EVKPAYATRY AITVWYFDAK ERAAARDKYQ LASGQKGVQV PVSQPTTPT
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

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.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 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. 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. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions. Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4.

Gene References into Functions

HS-induced PPARalpha-mediated downregulation of PHD1 is a novel pathway for PHD/HIF-1alpha transcriptional regulation. PMID:29500923
EglN2 might act as an FBW7 ubiquitin ligase substrate contributing to the progression of triple negative breast cancer. PMID:28036276
Selective reduction of PHD1 protein using CRISPR/Cas9 technology reduced both lipid peroxidation and mitochondrial impairment, and attenuated glutamate toxicity in the cultured neurons. PMID:27148687
Phd1 deficiency in dendritic cells significantly reduced interleukin-1beta production in response to lipopolysaccharide. Taken together, our results further support the development of selective PHD1 inhibitors for ulcerative colitis, and identify haematopoietic cells as their primary target. PMID:27981571
This study provides new information relating to the possible mechanism of therapeutic action of hydroxylase inhibitors that has been reported in pre-clinical models of intestinal and hepatic disease. PMID:27130823
PHD1 deficiency promotes hepatic steatosis and liver-specific insulin resistance but does not worsen the deleterious effects of HFD on metabolic homeostasis. PMID:27094951
These data identify PHD1 as a regulator of neuronal metabolism and a potential therapeutic target in ischemic stroke. PMID:26774962
PHD1 and PHD3 deletions promote angiogenesis in ischemia-injured tissue by increasing HIF1-alpha stability. PMID:25446011
Rosiglitazone increases PHD expression in a PPARgamma-dependent manner and that this leads to the commitment of anti-adipogenic proteins to the ubiquitination-proteasomal pathway and to the subsequent induction of adipocyte differentiation. PMID:24338020
PHD-1 deficient mouse appears to be the first animal model showing neuroepithelial bodies cell hyperplasia PMID:23080156
silencing of PHD-1 attenuates myocardial ischemia/reperfusion injury probably by enhancing HIF-1alpha/beta-catenin/endothelial nitric oxide synthase/nuclear factor-kappaB and Bcl-2 signaling pathway PMID:21083501
role for PHD1 as a positive regulator of intestinal epithelial cell apoptosis in the inflamed colon PMID:20600011
Loss of PHD1 provided tolerance of hepatocytes to acute hypoxia and protected them against ischemia/reperfusion damage. PMID:19818783
Deficiency or antagonism of oxygen sensor Phd1 induces hypoxia by reprogramming basal metabolism. PMID:18176562

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Subcellular Location

Nucleus.

Tissue Specificity

Highly expressed in testis, expression was also detected in the heart brain, liver kidney and lung. Expression was lowest in spleen and skeletal muscle. Constitutively expressed during differentiation of C2C12 skeletal myocytes.

Database Links

UNIGENE: Mm.29978

KEGG: mmu:112406

STRING: 10090.ENSMUSP00000078966

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