Recombinant Human Superoxide Dismutase 4/CCS protein is a Human Full Length protein, in the 1 to 274 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Delivers copper to copper zinc superoxide dismutase (SOD1).
Copper chaperone for superoxide dismutase, Superoxide dismutase copper chaperone, CCS
Recombinant Human Superoxide Dismutase 4/CCS protein is a Human Full Length protein, in the 1 to 274 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 1.16% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab99300 is purified using conventional chromatography techniques.
Delivers copper to copper zinc superoxide dismutase (SOD1).
In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.
Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241.
This product was previously labelled as Superoxide Dismutase 4.
Superoxide Dismutase 4 also known as CCS or Copper Chaperone for SOD1 plays a mechanical role as a copper chaperone for the antioxidant enzyme SOD1 (Superoxide Dismutase 1). With a molecular mass of approximately 30 kDa CCS assists in inserting copper into SOD1 activating it for its enzymatic function. CCS is expressed in various tissues including the brain liver and muscle facilitating its role wherever SOD1 activity is needed for protection against oxidative damage.
CCS contributes significantly to oxidative stress response by catalyzing the dismutation of superoxide radicals into less reactive molecular oxygen and hydrogen peroxide. This protein does not function independently but is part of a complex system involving SOD1 to mitigate oxidative damage within cells. CCS ensures SOD1 acquires the necessary copper which is essential for its dismutase activity hence playing a critical role in maintaining cellular health.
The copper delivery to SOD1 by CCS integrates into the broader antioxidant defense pathway. The copper chaperones like CCS link to pathways involving cellular copper homeostasis and oxidative stress management. The protein SOD1 which relies on CCS for copper addition also aligns with the apoptosis and neuroprotective pathways highlighting a shared role in cellular oxidation states control and maintaining neuronal integrity.
CCS associates with conditions such as Amyotrophic Lateral Sclerosis (ALS) and certain neurodegenerative disorders. These conditions relate to the malfunction of the antioxidant defense often involving misfolded SOD1 due to improper copper loading. The impairment in CCS’s role affects not just SOD1 but potentially other copper-dependent proteins exacerbating stress conditions and cellular vulnerability that characterizes these diseases.
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15% SDS-PAGE showing ab299300 (3μg).
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