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  4. Bovine Cu/Zn-Superoxide Dismutase,Cu/Zn-SOD ELISA Kit

Bovine Cu/Zn-Superoxide Dismutase,Cu/Zn-SOD ELISA Kit

  • 中文名称：
    牛铜锌-过氧化物岐化酶(Cu/Zn-SOD)酶联免疫试剂盒
  • 货号：
    CSB-E14090B
  • 规格：
    96T/48T
  • 价格：
    ￥4200/￥3000
  • 其他：

产品详情

  • 产品描述：

    This Bovine SOD1 ELISA Kit was designed for the quantitative measurement of Bovine SOD1 protein in serum, plasma. It is a Sandwich ELISA kit, its detection range is 15.6 ng/mL-1000 ng/mL and the sensitivity is 3.9 ng/mL.

  • 别名：
    SOD1 ELISA Kit; Superoxide dismutase [Cu-Zn] ELISA Kit; EC 1.15.1.1 ELISA Kit
  • 缩写：
  • Uniprot No.：
  • 种属：
    Bos taurus (Bovine)
  • 样本类型：
    serum, plasma
  • 检测范围：
    15.6 ng/mL-1000 ng/mL
  • 灵敏度：
    3.9 ng/mL
  • 反应时间：
    1-5h
  • 样本体积：
    50-100ul
  • 检测波长：
    450 nm
  • 研究领域：
    Metabolism
  • 测定原理：
    quantitative
  • 测定方法：
    Sandwich
  • 精密度：
    Intra-assay Precision (Precision within an assay): CV%<8%
    Three samples of known concentration were tested twenty times on one plate to assess.
    Inter-assay Precision (Precision between assays): CV%<10%
    Three samples of known concentration were tested in twenty assays to assess.
  • 线性度：
    To assess the linearity of the assay, samples were spiked with high concentrations of bovine Cu/Zn-SOD in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
    SampleSerum(n=4)
    1:1Average %97
    Range %92-104
    1:2Average %91
    Range %85-97
    1:4Average %90
    Range %88-95
    1:8Average %100
    Range %96-105
  • 回收率：
    The recovery of bovine Cu/Zn-SOD spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
    Sample TypeAverage % RecoveryRange
    Serum (n=5) 9087-94
    EDTA plasma (n=4)101103-105
  • 标准曲线：
    These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
    ng/mlOD1OD2AverageCorrected
    10002.014 2.115 2.065 1.929
    5001.537 1.640 1.589 1.453
    2501.201 1.108 1.155 1.019
    1250.878 0.844 0.861 0.725
    62.50.541 0.555 0.548 0.412
    31.20.342 0.329 0.336 0.200
    15.60.251 0.272 0.262 0.126
    00.137 0.135 0.136
  • 数据处理：
  • 货期：
    3-5 working days

产品评价

靶点详情

  • 功能：
    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
  • 基因功能参考文献：
    1. Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle. PMID: 30079537
    2. The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction PMID: 26872685
    3. SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability PMID: 25416864
    4. antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase, which show the changes in their expression during improper placental release PMID: 23398331
    5. Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis. PMID: 23101731
    6. ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows. PMID: 20072847
    7. Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced by PGF during functional luteolysis. PMID: 20519832
    8. At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase. PMID: 20682270
    9. Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo-monomer SOD-1 was calculated. PMID: 20411580
    10. flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa. The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution. PMID: 20516618
    11. expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles) PMID: 20197373
    12. Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions. PMID: 14688234
    13. Raman spectrum analysis strongly suggests that the His41-mediated hydrogen bond bridge of Cu-Zn superoxide dismutase plays a crucial role in keeping the protein structure suitable for highly efficient catalytic reactions. PMID: 15096035
    14. HCO(3)(-)-derived oxidant does not alter significantly the Cu(II) active site geometry and histidine coordination to Cu(II) in SOD1 as does H(2)O(2) alone PMID: 15123612
    15. copper- and carbonate radical anion-mediated oxidations have roles in hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation PMID: 15607903
    16. SOD1 mutants gain fatty acid binding abilities based on their structural instability and form cytotoxic granular aggregates PMID: 15799963
    17. The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA. PMID: 16202231
    18. Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). PMID: 17042490
    19. communication between the two monomers of SOD1 such that the binding of one zinc ion per homodimer has a more profound effect on the homodimeric protein structure than the binding of subsequent metal ions PMID: 17381088
    20. DNA accelerates the formation of SOD1 aggregates and is incorporated into SOD1 aggregates. SOD1 association with DNA, driven by electrostatic interactions, can restrict the orientation of SOD1 molecules and increase a SOD1 population along DNA strands. PMID: 17469801
    21. The results suggest that under cellular conditions ( approximately 5 mM bicarbonate) zinc-deficient SOD1 peroxidation could play a pathogenic role in neurodegenerative diseases. PMID: 17729118
    22. The expression of SOD1 and SOD2 through the course of the estrous cycle is reported. PMID: 18572235
    23. diminished hepatic protein nitration in the SOD1-/- mice was not directly related to plasma nitrite and nitrate concentrations PMID: 18573333
    24. DNAs tested are simultaneously condensed into a nanoparticle with a specific morphology during SOD1 aggregation, revealing that SOD1 aggregation and DNA condensation are two concurrent phenomena. PMID: 18690666
    25. Peroxymonocarbonate (HOOCO(2)(-)) is a key intermediate in the SOD1 peroxidase cycle and identify this species as the precursor of carbonate radical anions. PMID: 19286663

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  • 亚细胞定位：
    Cytoplasm. Nucleus.
  • 蛋白家族：
    Cu-Zn superoxide dismutase family
  • 数据库链接：