Recombinant Human TRP14 protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TRP14 also known as thioredoxin-related protein 14 functions as a redox-active protein. It has a molecular mass of approximately 14 kDa. Mechanically TRP14 catalyzes the reduction of disulfide bonds in proteins playing a role in maintaining cellular redox homeostasis. Its action depends on a CXXC motif in its active site which transfers electrons to disulfides. TRP14 expresses in various human tissues with notable levels in the heart and lungs.

Biological function summary

TRP14 impacts the cellular reduction-oxidation state participating in processes of cell growth and defense against oxidative stress. It does not typically form part of larger protein complexes but instead acts independently within the cell to exert its function. Through its catalytic activity TRP14 influences signaling events that dictate cellular response to harmful oxidative conditions.

Pathways

TRP14 integrates into the thioredoxin system which regulates redox-sensitive signaling pathways. These pathways involve proteins such as TRP32 and thioredoxin. The activity of TRP14 also contributes to the oxidative stress response pathway affecting the activation of downstream targets like Nrf2 a transcription factor that mediates antioxidant defense.

TRP14 shows connection to cancer and cardiovascular diseases. Its role in maintaining redox balance can influence tumor progression and cellular transformation processes in cancer. In cardiovascular diseases oxidative stress plays an important role and TRP14 through its interaction with other redox proteins like thioredoxin may modulate associated cellular damage contributing to disease pathology.