Recombinant Human TRP14 protein (Tagged) is a Human Full Length protein, in the 1 to 123 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
M A R Y E E V S V S G F E E F H R A V E Q H N G K T I F A Y F T G S K D A G G K S W C P D C V Q A E P V V R E G L K H I S E G C V F I Y C Q V G E K P Y W K D P N N D F R K N L K V T A V P T L L K Y G T P Q K L V E S E C L Q A N L V E M L F S E D
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.
TXNL5, TXNDC17, Thioredoxin domain-containing protein 17, 14 kDa thioredoxin-related protein, Protein 42-9-9, Thioredoxin-like protein 5, TRP14
Recombinant Human TRP14 protein (Tagged) is a Human Full Length protein, in the 1 to 123 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.
Belongs to the thioredoxin family.
The oxidized protein is reduced by TRXR1.
Previously labelled as TXNDC17.
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.
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.
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.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab236190.
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