Recombinant Human Extracellular superoxide dismutase [Cu-Zn](SOD3)

Code CSB-YP022399HU
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Source Yeast
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Code CSB-EP022399HU
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Source E.coli
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Code CSB-EP022399HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP022399HU
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Source Baculovirus
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Code CSB-MP022399HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names SOD3
Uniprot No. P08294
Alternative Names 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 Region 19-240
Target Protein Sequence WTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRV TGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVP HPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVEN GNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
Protein Length Extracellular domain
Tag Info The following tags are available.
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.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Function
Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Gene References into Functions
  1. High SOD3 expression is associated with cardiometabolic risk factors, and distal sensorimotor polyneuropathy. PMID: 29577557
  2. SOD3 might be a novel player in thyroid tumor stroma. PMID: 28216675
  3. 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
  4. Copper chaperone Atox-1 is involved in the induction of SOD3 in a monocyte cell line. PMID: 29168020
  5. 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
  6. 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
  7. 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
  8. 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
  9. The SOD3 enzyme plays a role in cardiovascular disease. PMID: 26901385
  10. SOD3 expression in human idiopathic pulmonary arterial hypertension is in part regulated by histone deacetylation. PMID: 27233998
  11. These data provide new insights into the functional actions of SOD3 on oxidative stress-induced cell damage. PMID: 27272114
  12. Study shows that patients with the Ala40Thr polymorphism in EC-SOD are at a higher risk of developing type 2 diabetes mellitus. PMID: 27966735
  13. Increased expression of SOD3 ameliorates H2O2-induced oxidative damage in neuroblastoma cells by inhibiting the mitochondrial pathway. PMID: 27084770
  14. 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
  15. 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
  16. FXR may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK activity. PMID: 25496033
  17. These results support the hypothesis that loss of extracellular SOD contributes to the invasive phenotype of pancreatic ductal adenocarcinoma PMID: 25634994
  18. The T-allele of rs2284659 in the promoter of SOD3 was associated with better cardiovascular outcomes in diabetic patients. PMID: 25855220
  19. SOD3 regulates the expression of multiple components of small G protein GTPase signal pathways. PMID: 25751262
  20. Expression of extracellular superoxide dismutase (EC-SOD) and expression of the prooxidant gene NADPH oxidase 4 was decreased significantly by trichostatin A. PMID: 25749103
  21. Extracellular superoxide dismutase ameliorates streptozotocin-induced rat diabetic nephropathy via inhibiting the ROS/ERK1/2 signaling. PMID: 26006040
  22. 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
  23. 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
  24. Sod3 is a critical mediator of VEGF-C-induced breast cancer metastasis. PMID: 25358638
  25. the rs1799895 polymorphism in extracellular superoxide dismutase affects cardiopulmonary disease risk by altering protein distribution PMID: 25085920
  26. 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
  27. No any significantly association between SOD3 rs2695232 polymorphism and seminal superoxide dismutase activity. PMID: 24658925
  28. 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
  29. Loss of SOD3 is associated with prostate cancer. PMID: 24922645
  30. Results suggest that there is no considerable influence of sequence variation in SOD3 on human longevity in Germans. PMID: 24146173
  31. 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
  32. 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
  33. The hEC-SOD protein was expressed in the egg white and showed antioxidant activity. PMID: 23977988
  34. 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
  35. Mesenchymal stem cell-derived chondrocytes, adipocytes, and osteocytes secrete an active and functional SOD3 enzyme. PMID: 22132904
  36. Overexpression of EC-SOD combined with neutrophil blockade protects transgenic mice from hyperoxia-induced lung injury. PMID: 22816678
  37. There is a positive relationship between the prolactinoma severity and serum EC-SOD. PMID: 23620962
  38. 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
  39. Antioxidant enzyme, SOD3, reverses DNA damage response and cellular transdifferentiation in aortic valve sclerosis. PMID: 23241403
  40. 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
  41. miR-21 promotes tumorigenesis and key targets of miR-21 in mediating this function were SOD3 and TNFalpha. PMID: 22836756
  42. 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
  43. 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
  44. The SOD3 might provide an effective strategy for the treatment of HAF-mediated skin inflammation. PMID: 21957979
  45. 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
  46. an alteration in SOD3 expression and activity could be associated to Systemic sclerosis (SSc) fibrosis. PMID: 22217996
  47. Mushroom lectin strongly prevented sodium arsenite-induced damage of SOD production pathway in hepatocytes. PMID: 21554548
  48. 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
  49. elevated sputum levels in smokers and in COPD patients PMID: 21621610
  50. Extracellular superoxide dismutase facilitates clearance of bacteria and limits inflammation in response to infection by promoting bacterial phagocytosis. PMID: 21641397

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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
Tissue Specificity Expressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.
Database Links

HGNC: 11181

OMIM: 185490

KEGG: hsa:6649

STRING: 9606.ENSP00000371554

UniGene: Hs.2420

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