Superoxide Dismutase 1 (SOD1) (NM_000454) Human Recombinant Protein

SKU
TP750141
Purified recombinant protein of Human superoxide dismutase 1, soluble (SOD1), full length, with N-terminal His tag, expressed in E. coli, 50ug
$261.00
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Proudly made in the USA
Specifications
Product Data
Species Human
Expression Host E. coli
Expression cDNA Clone or AA Sequence
Protein Sequence
A DNA sequence encoding human full-length SOD1
Tag N-His
Predicted MW 15.8 kDa
Concentration >0.05 µg/µL as determined by microplate BCA method
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer PBS, 10% glycerol
Note For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage Store at -80°C.
Stability Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Shipping Dry Ice
Reference Data
RefSeq NP_000445
Locus ID 6647
UniProt ID P00441
Cytogenetics 21q22.11
RefSeq Size 981
RefSeq ORF 462
Synonyms ALS; ALS1; HEL-S-44; homodimer; hSod1; IPOA; SOD; STAHP
Summary The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. In addition, this protein contains an antimicrobial peptide that displays antibacterial, antifungal, and anti-MRSA activity against E. coli, E. faecalis, S. aureus, S. aureus MRSA LPV+, S. agalactiae, and yeast C. krusei. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2020]
Protein Families Druggable Genome
Protein Pathways Amyotrophic lateral sclerosis (ALS), Huntington's disease, Prion diseases
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