Recombinant Human Egl Nine Homolog 2 (EGLN2) Protein (His)

Name: Recombinant Human Egl Nine Homolog 2 (EGLN2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10263P
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 2 (EGLN2) 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	Q96KS0
Target Symbol	EGLN2
Synonyms	DKFZp434E026; EGL nine (C.elegans) homolog 2; Egl nine homolog 2 (C. elegans); Egl nine homolog 2; EGLN 2; EGLN2; EGLN2_HUMAN; EIT 6; EIT6; Estrogen-induced tag 6; HIF P4H 1; HIF PH1; HIF prolyl hydroxylase 1; HIF-PH1; HIF-prolyl hydroxylase 1; HIFPH 1; HIFPH1; HPH 3; HPH-1; HPH-3; HPH3; Hypoxia inducible factor prolyl hydroxylase 1; Hypoxia-inducible factor prolyl hydroxylase 1; P4H1; PHD 1; PhD1; prolyl hydroxylase domain containing protein 1; Prolyl hydroxylase domain-containing protein 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT
Expression Range	283-407aa
Protein Length	Partial
Mol. Weight	18.1kDa
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	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.
Subcellular Location	Nucleus.
Database References	HGNC: 14660 OMIM: 606424 KEGG: hsa:112398 STRING: 9606.ENSP00000307080 UniGene: PMID: 29693343 Our study provided initial evidence that the insertion/deletion polymorphism rs10680577 may play a functional role in the development of CRC in the Chinese population PMID: 28218358 In advanced-stage Hodgkin's Lymphoma patients strong cytoplasmic PHD1 expression in Reed-Sternberg cells was associated with poor relapse-free survival among patients treated with involved-field radiotherapy and advanced-stage patients treated with doxorubicin, bleomycin, vinblastine and darcabazine and involved-field radiotherapy. PMID: 29277791 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 is phosphorylated by CDK2, CDK4 and CDK6 at Serine 130. PMID: 26644182 siRNA-mediated knockdown of PHD1 inhibited glucose-stimulated insulin secretion in pancreatic Beta cells. PMID: 26997627 EglN2 associates with the NRF1-PGC1alpha complex and controls mitochondrial function in breast cancer PMID: 26492917 rs3733829 in the EGLN2 gene is significantly associated with the risk of COPD in Chinese populations of Hainan province. PMID: 25609945 study conducted to investigate the association between gastric cancer (GC) susceptibility with a 4-bp insertion/deletion polymorphism (rs10680577) in the proximal promoter of EGLN2; findings showed that the heterozygote and the homozygote 4-bp del/del confer a significantly increased risk of GC PMID: 24517638 Data indicate that the prolyl hydrolase 1 (PHD1) rs10680577 polymorphism is associated with the risk of non-small cell lung cancer in a Chinese population. PMID: 24894671 PHD-1 played an important role in hypoxic response pathway of trophoblast through modulating the level of HIF-2alpha. PMID: 24644426 PHD1 could induce cell cycle arrest in lung cancer cells, resulting in the suppression of cell proliferation. PMID: 24935227 Results show that variants in two adjacent genes, EGLN2 and CYP2A6, influence smoking behavior related to disease risk. PMID: 24045616 Onconeuronal antigen Cdr2 correlates with HIF prolyl-4-hydroxylase PHD1 and worse prognosis in renal cell carcinoma. PMID: 23531419 Findings provided strong evidence for the hypothesis that rs10680577 contributes to hepatocarcinogenesis, possibly by affecting RERT-lncRNA structure and subsequently EGLN2 expression. PMID: 23026137 miR-205 serves a protective role against both oxidative and endoplasmic reticulum stresses via the suppression of EGLN2 and subsequent decrease in intracellular reactive oxygen species. PMID: 22859986 Principal component analysis of the covariance matrix of free AIRE-PHD1 highlights the presence of a "flapping" movement, which is blocked in an open conformation upon binding to H3K4me0. PMID: 23077531 PHD1 expression correlated with high proliferation, and these tumors were mainly estrogen receptor-negative. PMID: 21877141 Coexistence of PHD1 stabilized ATF4, as opposed to the destabilization of ATF4 by PHD3. PMID: 21951999 human prolyl hydroxylase might play an important role in determining the physiology and structure of the corpora lutea during the menstrual cycle and early pregnancy PMID: 20840881 role for PHD1 as a positive regulator of intestinal epithelial cell apoptosis in the inflamed colon PMID: 20600011 Prolyl hydroxylase-dependent (but hypoxia inducible factor HIF-1alpha and -2alpha-independent) activation of hypoxia-induced monocyte-endothelial adhesion assigns a new function to monocytic ICAM-1 under acute hypoxic conditions. PMID: 20574001 identified a human homolog of Caenorhabditis elegans Egl9 as a HIF prolyl hydroxylase PMID: 12351678 effect of WT or mutated VHL on PHD 1, 2, and 3 PMID: 15156561 defines the existence of two species of PHD1 and provide evidence that they are generated by alternative translational initiation PMID: 16509823 Understanding the mechanisms by which nickel can inhibit HIF-PHD's and stabilize HIF-1alpha may be important in the treatment of cancer and ischemic diseases. PMID: 16649251 Multiple mitochondrial products, including tricarboxylic acid intermediates and reactive oxygen species, can coordinate PHD activity, HIF stabilization, and cellular responses to O(2) depletion. PMID: 17101781 hypoxia releases repression of NFkappaB activity through decreased prolyl hydroxylase-dependent hydroxylation of IKKbeta PMID: 17114296 Results describe the expression, purification and characterization of the human prolyl hydroxylase PHD1 in Escherichia coli. PMID: 18710826 The identification of EGLN2 as a significantly deregulated gene that maps within the paired chromosome region directly implicates defects in the oxygen-sensing network to the biology of renal oncocytoma. PMID: 18773095 Overexpression of the oxygen sensor PHD-1 is associated with tumor aggressiveness in pancreatic endocrine tumors. PMID: 18927305 Authors identify an interaction between melanoma antigen-11 (MAGE-11) cancer-testis antigen and the major HIF-alpha hydroxylating enzyme PHD2. PMID: 19147576 Prolyl hydroxylase inhibitor reduced mitochondrial cytochrome c release, nuclear translocation of apoptosis inducing factor (AIF), and promoted Akt phosphorylation PMID: 19229863

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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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