biological source
human
Quality Level
recombinant
expressed in E. coli
assay
≥95% (SDS-PAGE and HPLC)
form
lyophilized powder
mol wt
31 kDa
technique(s)
cell culture | mammalian: suitable
color
white
application(s)
detection
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... SOD1(6647)
General description
Research Area: Cell Signaling
Cu/Zn superoxide dismutase (SOD1) is an intracellular antioxidant enzyme. A mature, functional human SOD1 is a relatively small (32 kDa) homodimeric metalloprotein.
Cu/Zn superoxide dismutase (SOD1) is an intracellular antioxidant enzyme. A mature, functional human SOD1 is a relatively small (32 kDa) homodimeric metalloprotein.
Recombinant Superoxide Dismutase I is fully biologically active when compared to standard.
Application
Superoxide Dismutase I human has been used to treat THP-1 (human leukemia monocytic cell line) or human primary macrophage cells to confirm signal specificity for superoxide.
Biochem/physiol Actions
Cu/Zn superoxide dismutase (SOD1) regulates basal levels of oxidative stress arising from the production of mitochondrial and cytosolic superoxide (O2 .−). Its high cytosolic abundance makes it unique from the other two human superoxide dismutases. SOD1 was believed to be a copper (Cu) storage protein, however, the crucial role of SOD1 is to act as an intracellular antioxidant. SOD1 also initiates gene transcription following exposure to neurotoxic stimuli and modulates signal transduction pathways involving reactive oxygen species (ROS). However, it is also implicated in multiple molecular mechanisms of cytotoxicity, contributing to pathology in diseases such as heart failure, cancer, diabetes, Down′s syndrome, amyotrophic lateral sclerosis (ALS), and Parkinson′s disease.
Preparation Note
Reconstitute in H2O to a concentration of ≥100 μg/ml. The solution can then be diluted into other aqueous buffers.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Superoxide dismutases.
I Fridovich
Annual review of biochemistry, 44, 147-159 (1975-01-01)
J S Pollock et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(23), 10480-10484 (1991-12-01)
The particulate enzyme responsible for the synthesis of endothelium-derived relaxing factor has been purified from cultured and native (noncultured) bovine aortic endothelial cells. Purification of the solubilized particulate enzyme preparation by affinity chromatography on adenosine 2',5'-bisphosphate coupled to Sepharose followed
S R Jolly et al.
Circulation research, 54(3), 277-285 (1984-03-01)
Therapy directed against the toxic effects of reactive oxygen species may reduce the final extent of ischemic injury in otherwise viable tissue irreversibly injured by the abrupt reoxygenation of reperfusion. In four groups of dogs, superoxide dismutase plus catalase (groups
全球贸易项目编号
| 货号 | GTIN |
|---|---|
| S9076-100UG | 04061833235386 |
