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AB84642

Recombinant Human Superoxide Dismutase 1 protein

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Recombinant Human Superoxide Dismutase 1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.

View Alternative Names

Superoxide dismutase [Cu-Zn], Superoxide dismutase 1, hSod1, SOD1

1 Images
SDS-PAGE - Recombinant Human Superoxide Dismutase 1 protein (AB84642)
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SDS-PAGE - Recombinant Human Superoxide Dismutase 1 protein (AB84642)

Key facts

Purity

>90% Densitometry

Expression system

Escherichia coli

Tags

Tag free

Applications

WB, SDS-PAGE

applications

Biologically active

No

Accession

P00441

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P00441","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Superoxide Dismutase 1 (SOD1) also known as Cu/Zn SOD or simply dismutase is an enzyme important for the detoxification of superoxide radicals. SOD1 catalyzes the conversion of two superoxide molecules into oxygen and hydrogen peroxide maintaining cellular redox balance. This enzyme typically exhibits a mass of approximately 32 kDa. SOD1 is expressed in the cytoplasm of cells throughout the body including tissues like liver kidney and brain.
Biological function summary

The enzyme functions as a homodimer with each subunit containing a copper and zinc ion. These metal ions are essential for the catalytic activity of SOD1 as the copper ion participates in electron transfer while the zinc ion provides structural stability. The enzyme protects cells from oxidative stress by neutralizing excess reactive oxygen species ensuring cellular health and functioning.

Pathways

SOD1 plays an important role in the cellular antioxidant defense system and is a part of the reactive oxygen species (ROS) metabolic pathway. It works in conjunction with catalase and glutathione peroxidase to limit oxidative damage within cells. The close interaction between these enzymes highlights the interdependence within the antioxidant defense network emphasizing their role in maintaining cellular homeostasis.

Mutations in the SOD1 gene are linked to familial Amyotrophic Lateral Sclerosis (ALS) a neurodegenerative condition. In ALS aberrant SOD1 proteins may lead to increased oxidative stress and motor neuron damage. Research also connects SOD1 to the pathogenesis of Alzheimer's disease where oxidative stress is a contributing factor. These associations underline SOD1's significance in neurodegenerative diseases highlighting potential therapeutic targets for interventions focused on oxidative stress management.
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Specifications

Form

Liquid

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General info

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Post-translational modifications

Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal degradation.. The ditryptophan cross-link at Trp-33 is responsible for the non-disulfide-linked homodimerization. Such modification might only occur in extreme conditions and additional experimental evidence is required.. Palmitoylation helps nuclear targeting and decreases catalytic activity.. Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.

Subcellular localisation

Mitochondrion

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Product protocols

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Target data

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
See full target information SOD1
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Product promise

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