Recombinant Mouse Egl Nine Homolog 3 Protein (EGLN3) Protein (His)

Name: Recombinant Mouse Egl Nine Homolog 3 Protein (EGLN3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08277P
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 Mouse Egl Nine Homolog 3 Protein (EGLN3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q91UZ4
Target Symbol	EGLN3
Synonyms	Egln3Egl nine homolog 3; EC 1.14.11.29; Hypoxia-inducible factor prolyl hydroxylase 3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; Prolyl hydroxylase domain-containing protein 3; PHD3; SM-20
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	PLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD
Expression Range	2-239aa
Protein Length	Full Length of Mature Protein
Mol. Weight	31.2kDa
Research Area	Others
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 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.
Subcellular Location	Nucleus. Cytoplasm.
Database References	KEGG: mmu:112407 STRING: 10090.ENSMUSP00000041874 UniGene: PMID: 28939592 PHD3 could protect against cardiac perivascular fibrosis and improve myocardial function in an obstructive sleep apnea mouse model by inhibiting endothelial-to-mesenchymal transition. PMID: 29051216 PHD3 expression induced by cytokines is NF-kappaB dependent in mesangial cells. Endogenously produced NO further augments PHD3 expression via HIF-1 alpha. PMID: 28054119 Opposing regulation and roles for PHD3 in lung dendritic cells and alveolar macrophages PMID: 28716863 Our observations disclose a novel role of PHD3 in the development of Tregs. PMID: 27331863 PHD3 is an active participant in atherogenesis PMID: 26995088 Cardiomyocyte-specific transgenic expression of PHD3 impairs the myocardial response to ischemia. PMID: 26044310 PHD3 protects intestinal epithelial barrier function and reveal a hydroxylase-independent function of PHD3 in stabilizing occludin PMID: 26124271 depletion of PHD3 leads to increased stabilization of HIF-1alpha and inhibition of DNA damage response, both of which may contribute to the cardioprotective effect seen with depletion of PHD3. PMID: 25633836 PHD3 loss sustains cell proliferation through the control of EGFR. PMID: 25420773 Using conditional PHD3-knockout mice, it was shown that PHD3 affects the production of Angptl2 and additionally influences the response toward this apoptosis-modulating factor. PMID: 24626957 ablation of the PHD3 gene resulted in increased angiogenesis and cardiac function after infarction thereby offering a potential target for management of ischemic myocardial disease PMID: 23978105 isoform-specific inhibition of Phd3 could be exploited to treat type 2 diabetes without the toxicity that could occur with chronic inhibition of multiple Phd isoforms. PMID: 24037093 Egln3 suppresses glioma progression PMID: 22905089 mice lacking PHD3 were resistant to the effects of ionizing radiation and had decreased thymic apoptosis, a biomarker of genomic integrity PMID: 22797300 It is concluded that impairment of PHD3 enzyme function aggravates the clinical course of abdominal sepsis PMID: 22786772 PHD3 has a role in regulating neutrophil survival in hypoxia PMID: 21317538 EGLN3 has a role in the regulation of NF-kappaB and suggests that it is involved in mediating myogenic differentiation, which is HIF-independent PMID: 20089853 PHD3 appears to be a tumor suppressor in colorectal cancer cells that inhibits IKKbeta/NF-kappaB signaling, independent of its hydroxylase activity. PMID: 19786027 Egln1/2/3 play dual roles in chondrocyted growth, acting as oxygen sensors and mediators of late stage events in the cell cycle. PMID: 17044072 the role of PHD3 in sympathoadrenal development extends beyond simple control of cell survival and organ mass, with functional PHD3 being required for proper anatomical and physiological integrity of the system PMID: 18332118 Phd3 loss exacerbates the HIF activation, hepatic steatosis, dilated cardiomyopathy, and premature mortality. PMID: 19720742

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.