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S9076

Sigma-Aldrich

Superoxide Dismutase I human

recombinant, expressed in E. coli

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About This Item

Numéro de classification (Commission des enzymes):
Numéro CE :
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Pureté

≥95% (SDS-PAGE and HPLC)

Forme

lyophilized powder

Poids mol.

31 kDa

Technique(s)

cell culture | mammalian: suitable

Couleur

white

Application(s)

detection

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... SOD1(6647)

Description générale

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.

Actions biochimiques/physiologiques

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.

Propriétés physiques

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.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
Distinct redox signalling following macrophage activation influences profibrotic activity
Lewis CV, et al.
Journal of immunology research (2019)

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