SOD1/Cu-Zn SOD Products

Description

FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. COFACTOR: Binds 1 zinc ion per subunit. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. DISEASE: Defects in SOD1 are the cause of familial amyotrophic lateral sclerosis (FALS); also called amyotrophic lateral sclerosis 1 (ALS1 or ALS). ALS is a degenerative disorder of motorneurons in the cortex, brainstem and spinal cord. ALS is characterized by muscular weakness and atrophy beginning in the hands and spreading to the forearms and legs. Muscle fasciculations are commonly visible. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. ALS is sometimes referred to as Lou Gehrig disease after the famous American baseball player who was diagnosed with the disorder. FALS, the familial form of ALS, accounts for about 10% of the cases and is transmitted in an autosomal dominant manner. The mean age at onset of FALS is 45 years. MISCELLANEOUS: Zinc binding promotes dimerization. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.

Bioinformatics

Entrez	20655 Mouse 24786 Rat 281495 Bovine 6647 Human
Uniprot	AAH01034 Human AAR21563 Human CAG46542 Human NM_000454 Human NM_000454.4 Human NP_000445.1 Human P00441 Human P00442 Bovine P22309 Human
Product By Gene ID	6647
Alternate Names	ALS ALS1 amyotrophic lateral sclerosis 1 (adult) Cu Cu/Zn superoxide dismutase EC 1.15.1.1 homodimer hSod1 indophenoloxidase A IPOA SOD SOD, soluble superoxide dismutase [Cu-Zn] Superoxide dismutase 1 superoxide dismutase 1, soluble Zn superoxide dismutase, EC 1.15.1.110superoxide dismutase, cystolic

Research Areas for SOD1/Cu-Zn SOD

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