Superoxide Dismutase from Human Erythrocyte, CAS No.9054-89-1

CAS: 9054-89-1 Cat. No.: np001016 EC Number: 232-943-0

GRADE & PURITY Bioactive, Native, ≥95%(SDS-PAGE), >50KU/mg protein; Pre-lyophilization Protein Concentration

Accession #

P04179,P00441,P08294

Bioactivity

>50KU/mg protein

Overview

Superoxide dismutases (SOD) are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. Three forms of SOD exist, based on the metal ions in the active site. These are Cu²⁺/Zn²⁺, Mn²⁺ and Fe²⁺ containing SOD. In vertebrate organisms, Cu/Zn-SOD is located in the cytoplasm as well as the mitochondrial intermembrane space, whereas Mn-SOD is located at the mitochondrial matrix space in prokaryotes. Fe-SOD is also found in prokaryotes and higher plants. Human erythrocyte SOD is a non-covalently bound homodimeric protein with two 16.3 kDa subunits containing 153 amino acids. Each dimer consists of two Cu²⁺ atoms and two Zn²⁺ atoms.
Application
Superoxide Dismutase from human erythrocytes has been used:
• to test its effect on human neutrophils in reactive oxygen species (ROS) measurement studies involving Pseudomonas aeruginosa infection.
• as an antioxidant to test its effect on ROS generation induced by atmospheric-pressure plasma jet (APPJ) in red blood cell (RBC) homogenates using optical spectroscopy studies
• to test its attenuating effect on hemoglobin (Hb)-induced nuclear factor-kappa B (NF- κB) and hypoxia-inducible factor (HIF) activity in human dermal microvascular endothelial cells (HMECs-1) 
• as a reference antioxidant protein to examine its expression in human intestinal Caco-2 cells following treatment with dietary flavonoids
• in combination with catalase to promote cell differentiation in vitro
Biochem/physiol Actions
Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
Mutations in the SOD1 gene are implicated in Amyotrophic lateral sclerosis (ALS).
Prepared from whole blood shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests. 
Aladdin products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research or further manufacturing use only.   

Specifications

Product Name

Superoxide Dismutase from Human Erythrocyte, CAS No.9054-89-1

Synonyms

SOD | Superoxide: superoxide oxidoreductase | SOD1 | SOD2 | SOD3 | ALS | ALS1 | IPOA | STAHP | hSod1 | HEL-S-44 | homodimer | GC1 | IPOB | IPO-B | MNSOD | MVCD6 | GClnc1 | Mn-SOD | lncRNA-GC1 | EC-SOD

Grade

Bioactive, Native

Specifications & Purity

Bioactive, Native, ≥95%(SDS-PAGE), >50KU/mg protein; Pre-lyophilization Protein Concentration

Biochemical and Physiological Mechanisms

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions.Multifunctional, involved in inflammation, angiogenesis, wound healing, reactive oxygen species (ROS) signaling, nitrous oxide (NO) signaling, apoptosis, senescence, aging, c

Bioactivity

>50KU/mg protein

Accession #

P04179, P00441, P08294

Predicted molecular weight

16 kDa

CAS

9054-89-1

Enzyme Commission Number

1.15.1.1

Molecule Type

Protein

Storage and Shipping

Shape

Lyophilized from 0.1 M potassium phosphate, pH 7.5

Concentration

>50KU/mg protein; Pre-lyophilization Protein Concentration

Reconstitution

After centrifugation, we suggest addition of de-ionized H2O to the original volume (See COA), followed by gentle mixingto ensure adequate homogenization. If further dilution is required, please use lyophilization buffer.

Storage

Store at -20°C,Avoid repeated freezing and thawing

Shipped In

Ice chest + Ice pads

Stability And Storage

Store at -20℃ long term (>1 year). Upon reconstitution, it is recommended to aliquot. Avoid freeze/thaw cycle.

Unit definition

One unit is defined as the amount of enzyme which will inhibit by 50% the formation of a colorimetric indicator by O2-in a xanthine/xanthine oxidase coupled system.

References

1. Dong Zhicheng, Xu Yunyun, Wu Can, Chao Jin, Tian Chen, Lin Zhang.  (2023)  Efficient removal of natural organo-chromium(III) through self-circulating decomplex and immobilization with nanoscale zero-valent iron.  Nano Research,      [PMID:] [10.1007/s12274-023-6028-9]

2. Jiayi Luo, Yunqiang Yi, Zhanqiang Fang.  (2023)  Nitrogen-rich magnetic biochar prepared by urea was used as an efficient catalyst to activate persulfate to degrade organic pollutants.  CHEMOSPHERE,      [PMID:37482309] [10.1016/j.chemosphere.2023.139614]

3. Jiayi Luo, Yunqiang Yi, Zhanqiang Fang.  (2023)  Effect of Mn-based magnetic biochar /PS reaction system on oxidation of metronidazole.  CHEMOSPHERE,      [PMID:37119924] [10.1016/j.chemosphere.2023.138747]

4. Gu Yurong, Zhang Yi, Jiang Chengchun, Dong Zijun, Bai Xue.  (2023)  Efficient metformin transformation in sulfite/UV process co-present with oxygen.  Frontiers in Environmental Science,      [PMID:] [10.3389/fenvs.2022.1071963]

5. Xixi Chen, Wanyi Fu, Zhichao Yang, Yulong Yang, Yanjun Li, Hui Huang, Xihui Zhang, Bingcai Pan.  (2023)  Enhanced H2O2 utilization efficiency in Fenton-like system for degradation of emerging contaminants: Oxygen vacancy-mediated activation of O2.  WATER RESEARCH,      [PMID:36603306] [10.1016/j.watres.2022.119562]

6. Xiang Li, Xianyi Gan.  (2022)  Photo-Fenton degradation of multiple pharmaceuticals at low concentrations via Cu-doped-graphitic carbon nitride (g-C3N4) under simulated solar irradiation at a wide pH range.  Journal of Environmental Chemical Engineering,      [PMID:] [10.1016/j.jece.2022.108290]

7. Jiayi Luo, Yunqiang Yi, Guangguo Ying, Zhanqiang Fang, Yifeng Zhang.  (2021)  Activation of persulfate for highly efficient degradation of metronidazole using Fe(II)-rich potassium doped magnetic biochar.  SCIENCE OF THE TOTAL ENVIRONMENT,      [PMID:34856267] [10.1016/j.scitotenv.2021.152089]

8. Zhenxiao Zheng, Kai Zhu, Zhiyuan Dai.  (2021)  Preparation of Antarctic Krill Oil Emulsion and Its Stability under Catalase Treatment.  Foods,  10  (11): (2797).  [PMID:34829078] [10.3390/foods10112797]

9. Qian Peng, Xuekun Tang, Kun Liu, Xianping Luo, Dongsheng He, Ying Dai, Ganghong Huang.  (2019)  High-Efficiency Catalysis of Peroxymonosulfate by MgO for the Degradation of Organic Pollutants.  Minerals,  10  (1): (2).  [PMID:] [10.3390/min10010002]

10. Shiyu Liu, Rongchang Wang, Cuixiang Ma, Dianhai Yang, Duanxin Li, Zbigniew Lewandowski.  (2019)  Improvement of electrochemical performance via enhanced reactive oxygen species adsorption at ZnO–NiO@rGO carbon felt cathodes in photosynthetic algal microbial fuel cells.  CHEMICAL ENGINEERING JOURNAL,      [PMID:] [10.1016/j.cej.2019.123627]

11. Yunqiang Yi, Guoquan Tu, Pokeung Eric Tsang, Zhanqiang Fang.  (2019)  Insight into the influence of pyrolysis temperature on Fenton-like catalytic performance of magnetic biochar.  CHEMICAL ENGINEERING JOURNAL,      [PMID:] [10.1016/j.cej.2019.122518]

12. Qing-Yuan Li, Xi-Wei Pang, Xing Xing, Xin-Xin Xu, Jun-Jun Jia, Ke-Jiang Zhao, Zhen-Bang Tian, Chao-Jun Wu, Zhong-Liang Zhang, Jing Wang.  (2025)  Facile synthesis of copper sulfide nanoflower decorated amine-grafted polyacrylonitrile fibers for rapid and long-lasting antimicrobial performance mediated by photothermal and photocatalytic effects.  Materials Today Communications,      [PMID:] [10.1016/j.mtcomm.2025.112201]

13. Maochang Xu, Dan Ran, Jian Hu, Jingying Mao, Dehui Qiao, Zongquan Zhang, Xiaoya Liang, Li Zhang, Yu Nie, Hong Yang, Xiangyu Zhou, Chunhong Li.  (2024)  Multifunctional Prussian blue nanozymes alleviate atherosclerosis through inhibiting the inflammation feedback loop.  Journal of Materials Chemistry B,      [PMID:39692245] [10.1039/D4TB01926A]