protein

Recombinant Human Cu/Zn Superoxide Dismutase Homodimer

MBS197057

0.02 mg

145 USD

Recombinant Protein

Recombinant Human Cu/Zn Superoxide Dismutase Homodimer

Cu/Zn Superoxide Dismutase Homodimer

superoxide dismutase; Superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; SOD, soluble; OTTHUMP00000107278; OTTHUMP00000107279; indophenoloxidase A; Cu/Zn superoxide dismutase; superoxide dismutase, cystolic; superoxide dismutase 1, soluble; Superoxide dismutase 1

SOD1; SOD1; ALS; SOD; ALS1; IPOA; hSod1; homodimer

SODC_HUMAN

E Coli

MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN

Human Cu/Zn Superoxide Dismutase Homodimer

Greater than 95% as determined by SDS- PAGE and RPHPLC.

Lyophilized white powder from a sterile-filtered solution (1mg/ml) in PBS, pH 7.4 Purified by proprietary chromatographic techniques.

Although lyophilized product is stable at room temperature for 3 weeks, it is best stored at or below -20 degree C. After reconstitution, product should be stored at or below -20 degree C. Addition of a carrier protein (such as 0.1% HSA or BSA) is recommended for long-term storage.

Solubility: Reconstitute lyophilized product in sterile distilled H2O to no less than 100ug/ml which can be further diluted in other aqueous solutions as needed.

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). Recombinant Human Cu/Zn SOD1 produced in E. coli is a homodimer nonglycosylated polypeptide chain containing 2 x 154 amino acids with a molecular weight of 31.6kDa.

4507149

NP_000445.1

NM_000454.4

P00441

15,936 Da

Amyotrophic Lateral Sclerosis (ALS) Pathway 83099!!Amyotrophic Lateral Sclerosis (ALS) Pathway 511!!FOXA1 Transcription Factor Network Pathway 137979!!Folate Metabolism Pathway 198833!!Formation Of Platelet Plug Pathway 106029!!Hemostasis Pathway 106028!!Huntington's Disease Pathway 83100!!Huntington's Disease Pathway 512!!Oxidative Stress Pathway 198916!!Peroxisome Pathway 131226

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. 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]

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. Ref.37Binds 1 zinc ion per subunit. Ref.37. Subunit structure: Homodimer; non-disulfide linked. Homodimerization may take place via the ditryptophan cross-link at Trp-33. The pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5, whereas wild-type protein does not. Ref.21 Ref.24 Ref.29 Ref.30 Ref.31 Ref.34 Ref.35 Ref.37 Ref.38. Subcellular location: Cytoplasm. Note: The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. Ref.80. Post-translational modification: 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 reponsible for the non-disulfide-linked homodimerization. Such modification might only occur in extreme conditions and additional experimental evidence is required. Involvement in disease: Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [. MIM:105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms. Ref.19 Ref.20 Ref.27 Ref.31 Ref.32 Ref.33 Ref.39 Ref.40 Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81. Miscellaneous: The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. Sequence similarities: Belongs to the Cu-Zn superoxide dismutase family.

0.02 mg

145 USD