TXN2 Yeast
Thioredoxin-2, TRX2, TRX-2, TXN-2, TXN2.
Description
Thioredoxin-2 Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 12.6kDa.
Product Specs
This product consists of the Thioredoxin-2 protein derived from yeast and produced in E. coli. It is a single polypeptide chain that lacks glycosylation and has a molecular weight of 12.6kDa.
Each milligram of TRX2 protein is supplied in a buffer solution containing 20mM phosphate at a pH of 7.4.
To reconstitute the lyophilized TXN2, it is recommended to dissolve it in sterile water with a resistance of 18 megaohms per centimeter (18MΩ-cm H2O).
TXN2 remains stable at 4 degrees Celsius for up to 3 weeks. For long-term storage, it is recommended to store the desiccated protein below -18 degrees Celsius to ensure optimal preservation. Repeated freeze-thaw cycles should be avoided.
TXN2 activity is measured by monitoring the absorbance change at a wavelength of 650 nm and a temperature of 25°C. This assay determines the enzyme's ability to catalyze redox reactions. The specific activity of this product was determined to be 3 units per milligram of protein.
Thioredoxin-2, TRX2, TRX-2, TXN-2, TXN2.
Product Science Overview
Thioredoxins contain a conserved active site with the sequence Cys-Gly-Pro-Cys, which is essential for their redox activity. The primary function of thioredoxins is to catalyze the reduction of disulfide bonds in proteins, thereby maintaining proteins in their reduced and functional state. This redox activity is crucial for various cellular processes, including:
- DNA Synthesis: Thioredoxins are involved in the first unique step of DNA synthesis by providing reducing equivalents to ribonucleotide reductase, the enzyme responsible for converting ribonucleotides to deoxyribonucleotides.
- Protein Folding: Thioredoxins assist in the formation of correct disulfide bonds during protein folding, ensuring that proteins achieve their proper three-dimensional structure.
- Regulation of Enzyme Activity: Thioredoxins regulate the activity of various enzymes through redox mechanisms, affecting processes such as cell proliferation and apoptosis.
In yeast, Thioredoxin-2 (TRX2) is encoded by the YLR043C gene. It is a single, non-glycosylated polypeptide chain with a molecular weight of approximately 12.6 kDa . TRX2 is involved in maintaining the redox state of the cytoplasm and participates in various cellular functions essential for the viability of yeast cells.
Recombinant yeast thioredoxin-2 is typically produced in Escherichia coli (E. coli) as a soluble protein. The recombinant protein is purified to a high degree of purity, often greater than 95%, as determined by reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) . The recombinant protein retains its enzymatic activity and can be used for various research applications.
Recombinant thioredoxin-2 has several applications in biotechnology and research:
- Biochemical Studies: It is used to study the redox mechanisms and interactions of thioredoxins with other proteins and enzymes.
- Drug Design: Thioredoxin-2 can be a target for drug design, especially in the context of pathogenic fungi such as Candida albicans . Inhibitors of thioredoxin reductase, the enzyme that regenerates reduced thioredoxin, are being explored as potential antifungal agents.
- Vaccine Development: Recombinant thioredoxin-2 can be used in the development of vaccines against fungal infections. For example, a recombinant thioredoxin reductase from Candida albicans has been shown to induce specific immune responses and reduce fungal burden in experimental models .
