Science
Mechanism of Action
On the skin, R-Escherichia coli Thioredoxin-1 functions primarily as a robust redox mediator. It actively reduces oxidized proteins through reversible thiol-disulfide exchange at its active site, which contains two redox-active cysteine residues (Cys32 and Cys35). This electron donation is critical for mitigating oxidative stress, notably by assisting peroxiredoxins in neutralizing hydrogen peroxide. Beyond its antioxidant capacity, it may offer anti-inflammatory benefits by modulating cytokine production, potentially soothing stressed or compromised skin.
Research
Clinical Evidence
Low confidenceN/A
Transparency
Dusting Analysis
The Formula
Formulation
Stability
This protein is water-soluble and stable across a broad pH range from 6.0 to 11.0. For optimal shelf-life, storage at -20°C or -80°C is recommended to prevent degradation, with careful avoidance of freeze-thaw cycles. The addition of 20-40% glycerol can enhance cryoprotection during storage, and the native protein exhibits high thermal stability up to 85°C.
Safety
Safety Profile
No specific safety assessments by the Cosmetic Ingredient Review (CIR), Scientific Committee on Consumer Safety (SCCS), or FDA for R-ESCHERICHIA COLI THIOREDOXIN-1 as a cosmetic ingredient were found, indicating an absence of specific safety guidelines or maximum concentration recommendations for topical use.
Your Skin
Skin Compatibility
Our Assessment
Verdict
While the fundamental biochemical mechanism of R-Escherichia coli Thioredoxin-1 suggests promising potential for redox regulation and anti-inflammatory effects in theory, there is currently insufficient specific safety and efficacy data for its use as a cosmetic ingredient.
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