Recombinant Rat Egl nine homolog 1 (Egln1)

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Egln1

Uniprot NO.

P59722

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

1-222

Target Protein Sequence

MNKHGICVVD DFLGRETGQQ IGDEVRALHD TGKFTDGQLV SQKSDSSKDI RGDKITWIEG KEPGCETIGL LMSSMDDLIR HCSGKLGNYR INGRTKAMVA CYPGNGTGYV RHVDNPNGDG RCVTCIYYLN KDWDAKVSGG ILRIFPEGKA QFADIEPKFD RLLFFWSDRR NPHEVQPAYA TRYAITVWYF DADERARAKV KYLTGEKGVR VELKPNSVSK DV
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

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

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.

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)

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 HIF1B. 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. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.

Gene References into Functions

PHD2 controls TNF-alpha effects by positively regulating NF-kappaB signaling, whereas NF-kappaB mediates cytokine-dependent PHD2 expression. PMID:25635047
PHD-2 KO mice showed significantly accelerated wound closure relative to WT. PMID:24695462
Impaired PHD2 response to high salt intake in the renal medulla may represent a novel mechanism for hypertension in Dahl S rats, and inhibition of PHD2 in the renal medulla could be a therapeutic approach for salt-sensitive hypertension. PMID:24190904
Renal medullary PHD2 is an important regulator in renal adaptation to high salt intake. PMID:22686466
PHD2 may directly interact with PDE4D to function as a novel regulator of the intracellular cAMP levels in cardiomyocytes. PMID:22975349
Data show that knockdown of PHD2, a major isoform of PHDs, by RNA interference reduced AT(1)R expression. PMID:21825224
High-salt intake inhibits PHD2 in the renal medulla, thereby upregulating the HIF-1alpha expression in rat renal medulla. PMID:20308610
identified the three forms of prolyl hydroxylase in rats and demonstrated that PHD2 has a role in proline hydroxylation, which regulates hypoxic preconditioning PMID:12876291
Decrease in PHD2 expression level is associated with ischemia. PMID:19349364