SOD1,Superoxide dismutase 1,hSod1
Human SOD1, His Tag (SO1-H5148) is expressed from E.coli cells. It contains AA Ala 2 - Gln 154 (Accession # AAH01034).
Predicted N-terminus: Met
This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 16.8 kDa. The protein migrates as 20 kDa under reducing (R) condition (SDS-PAGE).
Less than 1.0 EU per μg by the LAL method.
>97% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human SOD1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 97%.
Authors: Vehary Sakanyan et al.
Journal: Scientific Reports 2016
Application: In vitro binding assay
Superoxide dismutase [Cu-Zn] (SOD1) is also known as superoxide dismutase 1 (hSod1), an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 can bind copper and zinc ions and is one of three superoxide dismutases responsible for destroying free superoxide radicals in the body. The encoded isozyme (SOD1) is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide. Furthermore, the mutations of SOD1 gene can result in a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord.
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