Recombinant Human Extracellular Superoxide Dismutase [Cu-Zn] (SOD3) Protein (His)

Name: Recombinant Human Extracellular Superoxide Dismutase [Cu-Zn] (SOD3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02217P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Extracellular Superoxide Dismutase [Cu-Zn] (SOD3) 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	P08294
Target Symbol	SOD3
Synonyms	EC SOD; EC-SOD; Extracellular superoxide dismutase [Cu Zn]; Extracellular superoxide dismutase [Cu-Zn]; Extracellular superoxide dismutase; Extracellular superoxide dismutase precursor; MGC20077; SOD 3; SOD3; SODE_HUMAN; Superoxide Dismutase 3; Superoxide dismutase 3 extracellular
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	WTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
Expression Range	19-240aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.1kDa
Research Area	Cell Biology
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	Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Subcellular Location	Secreted, extracellular space. Golgi apparatus, trans-Golgi network. Note=99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.
Protein Families	Cu-Zn superoxide dismutase family
Database References	HGNC: 11181 OMIM: 185490 KEGG: hsa:6649 STRING: 9606.ENSP00000371554 UniGene: PMID: 29577557 SOD3 might be a novel player in thyroid tumor stroma. PMID: 28216675 SOD3 protects mesenchymal stem cells against the negative effects of serum deprivation via modulation of AMP-activated protein kinase/sirtulin 1, extracellular signalregulated kinase activation, and promoted Forkhead box O3a trafficking to the nucleus. PMID: 29921412 Copper chaperone Atox-1 is involved in the induction of SOD3 in a monocyte cell line. PMID: 29168020 the presence of terminal sialic acids in the N-glycans of EC-SOD enhanced both the secretion and furin-mediated C-terminal cleavage of EC-SOD. These results provide new insights into how the posttranslational modifications of EC-SOD control its functions. PMID: 29029079 SOD3 reduced HIF prolyl hydroxylase domain protein activity, which increased hypoxia-inducible factor-2alpha (HIF-2alpha) stability and enhanced its binding to a specific vascular endothelial cadherin promoter region. PMID: 29422508 EC-SOD released from activated neutrophils affects the redox conditions of the extracellular space and may offer protection against highly reactive oxygen species such as hydroxyl radicals otherwise generated as a result of respiratory burst activity of activated neutrophils. PMID: 27394172 The results of the present study demonstrate that TET1 might function as one of the key molecules in SOD3 expression through its 5mC hydroxylation in A549 cells. PMID: 28351182 The SOD3 enzyme plays a role in cardiovascular disease. PMID: 26901385 SOD3 expression in human idiopathic pulmonary arterial hypertension is in part regulated by histone deacetylation. PMID: 27233998 These data provide new insights into the functional actions of SOD3 on oxidative stress-induced cell damage. PMID: 27272114 Study shows that patients with the Ala40Thr polymorphism in EC-SOD are at a higher risk of developing type 2 diabetes mellitus. PMID: 27966735 Increased expression of SOD3 ameliorates H2O2-induced oxidative damage in neuroblastoma cells by inhibiting the mitochondrial pathway. PMID: 27084770 Results describe the molecular cloning of both full length and truncated form of human SOD3 both expressed in Sf9 insect cells as monomers and dimer conformation, with enzymatic activity. PMID: 26912083 study suggests that carriers of adiponectin gene promoter -11391G/A(AA) and EC-SOD (CG+GG) genotypes may have a high risk of nonalcoholic fatty liver disease (NAFLD), and the gene genotypes can interact with H. Pylori infection in the pathogenesis of NAFLD PMID: 27241145 FXR may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK activity. PMID: 25496033 These results support the hypothesis that loss of extracellular SOD contributes to the invasive phenotype of pancreatic ductal adenocarcinoma PMID: 25634994 The T-allele of rs2284659 in the promoter of SOD3 was associated with better cardiovascular outcomes in diabetic patients. PMID: 25855220 SOD3 regulates the expression of multiple components of small G protein GTPase signal pathways. PMID: 25751262 Expression of extracellular superoxide dismutase (EC-SOD) and expression of the prooxidant gene NADPH oxidase 4 was decreased significantly by trichostatin A. PMID: 25749103 Extracellular superoxide dismutase ameliorates streptozotocin-induced rat diabetic nephropathy via inhibiting the ROS/ERK1/2 signaling. PMID: 26006040 ECSOD Ala40Thr polymorphism, a significant association was observed between this polymorphism and HCC risk in non-hepatitis B virus (HBV) carriers but not in HBV carriers PMID: 25894370 The combination of serum S100A9, SOD3, and MMP9 levels could achieve 92.5% sensitivity and 95% specificity to discriminate between pulmonary tuberculosis and healthy controls. PMID: 25332062 Sod3 is a critical mediator of VEGF-C-induced breast cancer metastasis. PMID: 25358638 the rs1799895 polymorphism in extracellular superoxide dismutase affects cardiopulmonary disease risk by altering protein distribution PMID: 25085920 The treatment with E2 suppressed, whereas VC and Res prevented E2-mediated decrease in the expression levels of SOD3, NQO1, Nrf2 mRNA, and protein in MCF-10A cells PMID: 25130429 No any significantly association between SOD3 rs2695232 polymorphism and seminal superoxide dismutase activity. PMID: 24658925 These results demonstrate that the transcription factor HIF-1alpha and its important gene target VEGF can be modulated by the antioxidant enzyme EcSOD. PMID: 24509158 Loss of SOD3 is associated with prostate cancer. PMID: 24922645 Results suggest that there is no considerable influence of sequence variation in SOD3 on human longevity in Germans. PMID: 24146173 the impact of Glutamate carboxypeptidase II (GCPII) haplotypes on the expression of PSMA, BNIP3, Ec-SOD, GSTP1 and RASSF1 genes were elucidated to understand the epigenetic basis of oxidative stress and prostate cancer risk. PMID: 23979608 Data suggest that epigenetic silencing of EcSOD may contribute to mammary tumorigenesis and that restoring the extracellular superoxide scavenging activity could be an effective strategy for breast cancer treatment. PMID: 23318435 The hEC-SOD protein was expressed in the egg white and showed antioxidant activity. PMID: 23977988 The less common allele in SOD3 rs699473 was associated with an increased risk of high-grade prostate cancer (T > C: OR = 1.40, 95% CI: 1.04-1.89). PMID: 24038157 Mesenchymal stem cell-derived chondrocytes, adipocytes, and osteocytes secrete an active and functional SOD3 enzyme. PMID: 22132904 Overexpression of EC-SOD combined with neutrophil blockade protects transgenic mice from hyperoxia-induced lung injury. PMID: 22816678 There is a positive relationship between the prolactinoma severity and serum EC-SOD. PMID: 23620962 results suggest aberrations in one-carbon metabolism appear to induce altered gene expression of EC-SOD, GSTP1, and BNIP3, and thus contribute to the increased oxidative stress and increased susceptibility to coronary artery disease PMID: 23160801 Antioxidant enzyme, SOD3, reverses DNA damage response and cellular transdifferentiation in aortic valve sclerosis. PMID: 23241403 studies further demonstrate that SOD3, but not SOD2 and SOD1, is induced by antioxidants and is regulated through NRF2; SOD3 may thus be an important gene in defense against oxidative stress and in the prevention of estrogen-mediated breast cancer PMID: 23027624 miR-21 promotes tumorigenesis and key targets of miR-21 in mediating this function were SOD3 and TNFalpha. PMID: 22836756 results suggest that the expression of Extracellular-superoxide dismutase (EC-SOD)was increased by TPA administration, and it was speculated that the activation of PKC, MEK/ERK and an increase of intracellular ROS were necessary for the induction of EC-SOD in THP-1 cells PMID: 22313459 There were no significant differences in the distribution of the different genotypes or allele gene frequencies in the EC-SOD genes between the patients and the controls. PMID: 21781513 The SOD3 might provide an effective strategy for the treatment of HAF-mediated skin inflammation. PMID: 21957979 The loss of EcSOD expression is unique among the superoxide dismutases in lung cancer and is the result of EcSOD promoter methylation and LOH, suggesting that its early loss may contribute to ECM remodeling and malignant progression. PMID: 22064654 an alteration in SOD3 expression and activity could be associated to Systemic sclerosis (SSc) fibrosis. PMID: 22217996 Mushroom lectin strongly prevented sodium arsenite-induced damage of SOD production pathway in hepatocytes. PMID: 21554548 Extracellular superoxide dismutase cell-specific and interferon-gamma-inducible expression in pulmonary artery cells is regulated, to a major degree, by epigenetic mechanisms that include histone acetylation and DNA methylation. PMID: 21493784 elevated sputum levels in smokers and in COPD patients PMID: 21621610 Extracellular superoxide dismutase facilitates clearance of bacteria and limits inflammation in response to infection by promoting bacterial phagocytosis. PMID: 21641397

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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.