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Recombinant Human Cu/Zn Superoxide Dismutase Homodimer

$883.00

Host Quantity Applications Species Reactivity Data Sheet  
1000ug WB Human
SKU: 13002P-1000 Categories: ,
Overview
Product Name Cu/Zn Superoxide Dismutase Homodimer (13002P-1000)
Description Recombinant Human Cu/Zn SOD1 produced in E. coli is a homodimer non-glycosylated polypeptide chain containing 2 x 154 amino acids with a molecular weight of 31.6kDa.
Target Cu/Zn Superoxide Dismutase Homodimer
Product Background Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. It protects a cell from dangerous levels of superoxide. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis (ALS).
Species Reactivity Human
Applications WB
Source Escherichia coli
Properties
Form Lyophilized
Concentration Lot Specific
Formulation Lyophilized from a sterile-filtered solution (1mg/ml) in PBS, pH 7.4
Buffer Formulation PBS
Buffer pH pH 7.4
Purity Greater than 95% as determined by SDS- PAGE and RP-HPLC
Specificity Information
Target Name Superoxide dismutase [Cu-Zn]
Target ID Cu/Zn Superoxide Dismutase Homodimer
Alternative Names SOD1
Sequence Location Cytoplasm , Mitochondrion , Nucleus , Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria.
Sequence MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ
Biological Activity Cu/Zn Superoxide Dismutase Homodimer
Biological Function Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {PubMed:24140062}.
Background Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. It protects a cell from dangerous levels of superoxide. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis (ALS).
Application Images
Additional Information
Handling
Storage Store at 2 - 8ºC. Do not Freeze.
Dilution Instructions Reconstitute lyophilized product in sterile distilled H2O to no less than 100ug/ml which can be further diluted in other aqueous solutions as needed.
References & Data Sheet