| Size | Price | |
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| 1mg | ||
| 5mg | ||
| 10mg | ||
| Other Sizes |
| Targets |
The peptide targets the thioredoxin reductase (TrxR) enzyme, which is a critical component of the thioredoxin system. TrxR catalyzes the reduction of thioredoxin, which in turn reduces disulfide bonds in various target proteins, thereby regulating numerous cellular processes including antioxidant defense, DNA synthesis, and cell proliferation. The specific 53-67 region of TrxR is involved in the enzyme's structural integrity and catalytic activity. This peptide may interfere with or help characterize TrxR function, particularly in the context of the enzyme's selenocysteine-containing active site.
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| ln Vitro |
In vitro studies using this peptide have been conducted to understand its role in modulating the activity of thioredoxin reductase. The peptide can be used to investigate competitive inhibition of TrxR or to study binding interactions with the full-length enzyme. Standard in vitro activity assays measure the reduction of insulin disulfides or the chromogenic substrate 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) in the presence of NADPH. While the peptide itself is not a potent inhibitor, it serves as a valuable tool for mapping functional domains within the TrxR protein and studying protein-protein recognition mechanisms in the thioredoxin system.
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| ln Vivo |
In vivo activity studies for this peptide typically involve animal models of oxidative stress-related diseases, such as ischemia-reperfusion injury, neurodegenerative disorders, or inflammatory conditions. When administered, the peptide may influence cellular redox status by interfering with the thioredoxin system. However, as with most peptide-based research tools, in vivo efficacy can be limited by rapid proteolytic degradation and poor bioavailability, often necessitating formulation modifications or alternative administration routes to achieve measurable effects in live animal models.
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| Enzyme Assay |
Binding studies for thioredoxin reductase peptide can be performed using surface plasmon resonance (SPR) to measure the interaction between the peptide and purified TrxR or other binding partners. Enzyme activity assays using purified TrxR in buffer containing NADPH and a disulfide substrate can be employed to assess whether the peptide influences catalytic activity. Typical reaction conditions include 100 mM potassium phosphate buffer (pH 7.0), 2 mM EDTA, and 0.2 mM NADPH at 25degC or 37degC. Inhibition constants (Ki) can be determined by varying peptide concentrations and measuring the change in enzymatic activity.
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| Cell Assay |
For cell-based experiments, the peptide is typically dissolved in an appropriate solvent (such as PBS or cell culture medium) and added to cultured cells at concentrations ranging from 1-100 uM depending on the experimental design. Cells are incubated with the peptide for various durations (e.g., 4-48 hours) to assess effects on cellular redox status, viability, or specific signaling pathways. Downstream analyses may include measurements of reactive oxygen species (ROS) levels using fluorescent probes (e.g., DCFH-DA), assessment of apoptosis markers, or Western blotting to evaluate changes in the expression of proteins involved in antioxidant defense pathways.
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| Animal Protocol |
Animal studies using this peptide typically employ rodent models (mice or rats). The peptide can be administered via intraperitoneal (IP) or intravenous (IV) injection at doses typically ranging from 1-20 mg/kg, depending on the study objectives. For repeated dosing regimens, administrations may be performed daily or every other day over a period of 1-4 weeks. Control groups receive vehicle (e.g., PBS or saline). Endpoints include measurement of tissue TrxR activity, assessment of oxidative stress biomarkers (malondialdehyde, glutathione levels), histopathological examination of target organs, and evaluation of disease-specific parameters in models of oxidative stress-related conditions.
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| ADME/Pharmacokinetics |
Pharmacokinetic data specifically for thioredoxin reductase peptide TFA are not extensively characterized. As a peptide of 15 amino acids (molecular weight approximately 1618 Da), it is likely subject to rapid proteolytic degradation in biological fluids, typically resulting in a short plasma half-life (likely minutes to a few hours). Peptides of this size are generally cleared primarily via renal filtration and enzymatic degradation. The TFA salt form is used to enhance solubility and stability during storage. Bioavailability after oral administration is expected to be very low due to poor absorption and extensive first-pass metabolism.
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| Toxicity/Toxicokinetics |
General toxicity considerations for peptide research tools: At standard research concentrations (1-100 uM in vitro or 1-20 mg/kg in vivo), the peptide is generally well-tolerated. The primary safety consideration relates to potential off-target effects on the thioredoxin system, which plays essential roles in cellular redox balance. Since thioredoxin reductase is a selenoprotein essential for cell viability, complete inhibition could be toxic. However, as this peptide is a fragment rather than a potent inhibitor, significant toxicity is unlikely at typical research doses. Standard laboratory safety practices for handling peptides and TFA salts should be followed.
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| References |
[1]. Jan YH, et al. Cross-linking of thioredoxin reductase by the sulfur mustard analogue mechlorethamine(methylbis(2-chloroethyl)amine) in human lung epithelial cells and rat lung: selective inhibition of disulfide reduction but not redox cycling. Chem Res To
[2]. Valette O, et al. Biochemical Function, Molecular Structure and Evolution of an Atypical Thioredoxin Reductase from Desulfovibrio vulgaris. Front Microbiol. 2017 Sep 29;8:1855. |
| Additional Infomation |
Thioredoxin reductase is part of the broader antioxidant defense network that includes glutathione, peroxiredoxins, and superoxide dismutases. This peptide (residues 53-67) is located in the N-terminal domain of TrxR, which contains the redox-active Cys59-Cys64 pair. TrxR is unique among antioxidant enzymes as it is the only known enzyme that reduces thioredoxin using NADPH. Dysregulation of the thioredoxin system has been implicated in various pathologies including cancer (where TrxR is often overexpressed), neurodegenerative diseases (associated with increased oxidative stress), and cardiovascular diseases. Thus, this peptide serves as a valuable research tool for understanding TrxR biology and developing therapeutic strategies targeting the thioredoxin system, though it has not itself progressed to clinical trials or received regulatory approval.
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| Molecular Formula |
C68H107F3N18O20S2
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|---|---|
| Related CAS # |
Thioredoxin reductase peptide;950890-23-0
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| Appearance |
Light yellow to yellow solid powder
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: Please store this product in a sealed and protected environment, avoid exposure to moisture. |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
DMSO :~50 mg/mL (~30.91 mM)
H2O :~12.5 mg/mL (~7.73 mM) |
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| Solubility (In Vivo) |
Solubility in Formulation 1: ≥ 2.5 mg/mL (1.55 mM) (saturation unknown) in 10% DMSO + 40% PEG300 + 5% Tween80 + 45% Saline (add these co-solvents sequentially from left to right, and one by one), clear solution.
For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 400 μL PEG300 and mix evenly; then add 50 μL Tween-80 to the above solution and mix evenly; then add 450 μL normal saline to adjust the volume to 1 mL. Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH₂ O to obtain a clear solution. Solubility in Formulation 2: ≥ 2.5 mg/mL (1.55 mM) (saturation unknown) in 10% DMSO + 90% (20% SBE-β-CD in Saline) (add these co-solvents sequentially from left to right, and one by one), clear solution. For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 900 μL of 20% SBE-β-CD physiological saline solution and mix evenly. Preparation of 20% SBE-β-CD in Saline (4°C，1 week): Dissolve 2 g SBE-β-CD in 10 mL saline to obtain a clear solution. View More
Solubility in Formulation 3: ≥ 2.5 mg/mL (1.55 mM) (saturation unknown) in 10% DMSO + 90% Corn Oil (add these co-solvents sequentially from left to right, and one by one), clear solution. |
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
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