Recombinant Human Egl Nine Homolog 1 (EGLN1) Protein (His)

Name: Recombinant Human Egl Nine Homolog 1 (EGLN1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07606P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Egl Nine Homolog 1 (EGLN1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9GZT9
Target Symbol	EGLN1
Synonyms	(Hypoxia-inducible factor prolyl hydroxylase 2)(HIF-PH2)(HIF-prolyl hydroxylase 2)(HPH-2)(Prolyl hydroxylase domain-containing protein 2)(PHD2)(SM-20)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF
Expression Range	177-426aa
Protein Length	Partial
Mol. Weight	31.9 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 1232 OMIM: 606425 KEGG: hsa:54583 STRING: 9606.ENSP00000355601 UniGene: PMID: 28900510 In vitro studies showed that a complement C1q-A chain peptide is not a substrate for PHD2 but is a substrate for CP4H1. PMID: 28506759 GPT2 reduced alpha-ketoglutarate level in cells leading to the inhibition of proline hydroxylase 2 (PHD2) activity involved in the regulation of HIF1alpha stability. Accumulation of HIF1alpha, resulting from GPT2-alpha-ketoglutarate-PHD2 axis, constitutively activates sonic hedgehog (Shh) signaling pathway. PMID: 28839461 Studied the association between SNPs around the EGLN1 genomic region, possibly involved in high-altitude adaptation, and physiological changes to hypobaric hypoxia exposure in a cohort of Japanese lowlanders. PMID: 29625625 the expression of prolyl hydroxylase domain 2 (PHD2) is selectively increased in CKD-AT-MSCs and its inhibition can restore the expression of HIF-1alpha and the wound healing function of CKD-AT-MSCs. These results indicate that more studies about the functions of MSCs from CKD patients are required before they can be applied in the clinical setting PMID: 28537846 Functionally active PHD2 SNP rs516651 [18], located in the key pathway for the hypoxic-inflammatory response, is associated with increased 30-day mortality in Acute Respiratory Distress Syndrome (ARDS) patients. In contrast, the PHD2 SNP rs480902 is not. Furthermore, the HIF-2alpha SNP [ch2: 46441523(hg18)] GG-genotype was neither present in our ARDS patients of Caucasian heritage nor in healthy Caucasian blood donors. PMID: 28613249 We genotyped 347 Tibetan individuals from varying altitudes for both the Tibetan-specific EGLN1 haplotype and 10 candidate SNPs in the EPAS1 haplotype and correlated their association with hemoglobin levels. PMID: 28233034 PHD2 is a direct binding partner of EGFR and show that PHD2 regulates EGFR stability as well as its subsequent signaling in breast carcinoma cells. PMID: 28038470 A mechanism of PHD2 regulation that involves the mTOR and PP2A pathways. PMID: 28199842 These data unravel B55alpha as a PHD2 substrate and highlight a role for PHD2-B55alpha in the response to nutrient deprivation. PMID: 28329677 miR-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating HIF-1alpha/VEGF pathway. PMID: 27030384 Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen stores is linked to the resolution of neutrophil-mediated inflammatory responses PMID: 28805660 prolyl hydroxylase 2 plays an important tumor suppressive role in liver cancer PMID: 27307407 Genetic variants in HIF-1alpha and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis PMID: 27515179 Results identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function. PMID: 27795296 Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases. PMID: 27502280 The role of PHD-2 in breast cancer [review] PMID: 26951539 Sulfur mustard negatively affects hypoxia-stimulated HIF-1alpha signaling in keratinocytes and fibroblasts and thus possibly contributes to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors. PMID: 26082309 The HIFalpha subunit is usually prolyl-hydroxylated by EglN family members under normoxic conditions, causing its rapid degradation. Study confirmed that triple-negative breast cancer cells secrete glutamate, which is both necessary and sufficient for the paracrine induction of HIF1alpha in such cells under normoxic conditions. PMID: 27368101 Disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha and aerobic glycolysis in response to oxidative stress. PMID: 26740011 The present study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least in part, via the regulation of the PHD2/HIF-1alpha signaling pathway. PMID: 26676934 the levels of both miR-182 and HIF1alpha were elevated, while the expression PHD2 and FIH1 was downregulated in a mouse model of prostate cancer. PMID: 26205124 findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF) activation PMID: 26323721 In this article, UTMD/PEI mediated gene transfection was investigated and the US parameters were optimized. Furthermore, the biological effects of PHD2 shRNA were investigated in H9C2 cells. PMID: 26267649 a genetic link between EGLN1 and VWF in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported. PMID: 26047609 Data show that dimethyl-2-ketoglutarate (DKG) inhibits hypoxia-inducible factor 1alpha (HIF-1alpha) proline hydroxylation and degradation mediated by prolyl-4-hydroxylase PHD2. PMID: 25420025 striking enrichment of high-altitude ancestry in the Tibetan genome, indicating that migrants from low altitude acquired adaptive alleles from the highlanders PMID: 24513612 The kinetic properties of PHD2 and FIH with respect to oxygen reflect their cellular hypoxia-sensing ability. PMID: 26112411 Germ-line PHD1 and PHD2 mutations detected in patients with pheochromocytoma/paraganglioma-polycythemia PMID: 25263965 The association between EGLN1 and HIF-1AN single nucleotide polymorphisms and acute mountain sickness in a Han Chinese population, was examined. PMID: 25431923 Compared to those with high PHD2 expressions, patients with low PHD2 expression had significantly longer DFS and OS periods. PMID: 25546659 PHD2 inhibits the adaptation of glioblastoma cells to hypoxia by regulating the expression of HIF-alpha subunits. PMID: 25010988 higher expression in normal skin compared to seborrheic keratosis, Bowen's disease and cutaneous squamous cell carcinoma PMID: 24354513 Regulation and expression of both PHD2 and HIF-1a are important to the biology of sarcomas, and loss of PHD2 function has an additional adverse effect in the prognosis of sarcomas in tumors expressing HIF-1a. PMID: 20026900 Data indicate that the Tibetan prolyl hydroxylase domain protein 2 (PHD2) haplotype (D4E/C127S) strikingly diminishes the interaction of PHD2 with heat shock protein 90 co-chaperone protein p23 (prostaglandin E synthase). PMID: 24711448 The diminished expression of PHD1 and PHD2 and elevated level of FIH protein in cancerous tissue compared to histopathologically unchanged colonic mucosa was not associated with DNA methylation within the CpG islands of the PHD1, PHD2 and FIH genes. PMID: 24195777 results demonstrate that HIF-1alpha transcription and protein synthesis are controlled by TGF-beta1/Smad3 signaling, whereas HIF-1alpha protein stability is controlled by PHD2, which is regulated by TGF-beta1/Smad3 signaling. PMID: 23088526 EGLN1 contributes to the adaptively low hemoglobin level of Tibetans compared with acclimatized lowlanders at high altitude. PMID: 23666208 PHD2 regulates and hydroxylates HIF-1alpha by binding to its C-terminal domain. PMID: 23787140 These studies formally prove that a missense mutation in PHD2 is the cause of the erythrocytosis, show that this occurs through haploinsufficiency, and point to multifactorial control of red cell mass by PHD2. PMID: 24121508 the N-terminal region of C16 is predicted to have a PHD2-like structural fold but lacks the catalytic active site residues of PHDs PMID: 23836663 PHD2 silencing promotes adipose-derived stem cell survival in infarcted myocardia. PMID: 23694817 HIF-specific hydroxylase PHD-2 may represent a relevant target for cartilage repair. PMID: 23334958 Knockdown of prolyl-4-hydroxylase domain 2 inhibits tumor growth of human breast cancer MDA-MB-231 cells by affecting TGF-beta1 processing. PMID: 23225569 PHD2-mediated hydroxylation of HIF-1alpha predominantly occurs in the cell nucleus and is dependent on very dynamic subcellular trafficking of PHD2. PMID: 22946054 p23 recruits PHD2 to the HSP90 machinery to facilitate HIF-1alpha hydroxylation PMID: 23413029 a unique mechanism for the regulation of HIF-1alpha stability that involves ERbeta-mediated transcriptional regulation of PHD2 and they highlight an unexpected role for PHD2 in maintaining epithelial differentiation. PMID: 23487784 The study scrutinizes the unfolding pathways of the PHD2 catalytic domain's possible species and demonstrates the properties of their unfolding states by computational approaches. PMID: 23077544 PHD2 may directly interact with PDE4D to function as a novel regulator of the intracellular cAMP levels in cardiomyocytes. PMID: 22975349 prevalence of the risk alleles in high altitude pulmonary edema and the protective alleles in healthy Lakakhi highland natives have provided us with allelic variants at the same locus that are involved in disease and adaptation PMID: 23130672

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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