Skip to Content
MilliporeSigma
All Photos(1)

Documents

S9076

Sigma-Aldrich

Superoxide Dismutase I human

recombinant, expressed in E. coli

Sign Into View Organizational & Contract Pricing


About This Item

Enzyme Commission number:
EC Number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

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.

Physical properties

Recombinant Superoxide Dismutase I is fully biologically active when compared to standard.

Reconstitution

Reconstitute in H2O to a concentration of ≥100 μg/ml. The solution can then be diluted into other aqueous buffers.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Superoxide dismutases.
I Fridovich
Annual review of biochemistry, 44, 147-159 (1975-01-01)
S J Collins et al.
The Journal of experimental medicine, 149(4), 969-974 (1979-04-01)
The HL-60 human promyelocytic leukemia cell line can be induced to terminally differentiate to mature myeloid cells sharing a number of functional characteristics with normal granulocytes including response to chemoattractants, development of complement receptors, phagocytosis, superoxide production, and nitroblue tetrazolium
Distinct redox signalling following macrophage activation influences profibrotic activity
Lewis CV, et al.
Journal of immunology research (2019)
Superoxide dismutase 1 in health and disease: how a frontline antioxidant becomes neurotoxic
Trist BG, et al.
Angewandte Chemie (International Edition in English), 60(17), 9215-9246 (2021)
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service