TXN Mouse
Escherichia Coli.
TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
Description
TXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Thioredoxin, also known as TRX, is a ubiquitous protein with a crucial role in redox reactions. It features a single disulfide active site within a conserved Cys-Gly-Pro-Cys motif, enabling it to function as a general protein disulfide oxidoreductase. Thioredoxin participates in various cellular processes, including DNA synthesis, by interacting with a wide array of proteins through a reversible redox mechanism involving the oxidation of two cysteine thiol groups to a disulfide. This process involves the transfer of two electrons and two protons, effectively interconverting a disulfide and a dithiol. Due to its efficient oxidoreductase activity, thioredoxin is believed to contribute to proper protein folding by facilitating the formation of correct disulfide bonds.
Recombinant Mouse Thioredoxin (TXN), produced in E. coli, is available as a single, non-glycosylated polypeptide chain. This 128-amino acid protein encompasses residues 1-105 of the native TXN sequence and incorporates a 23-amino acid His-tag at the N-terminus. The molecular weight of the recombinant TXN protein is 14.1 kDa. Purification is achieved through proprietary chromatographic methods.
The product appears as a clear, colorless solution that has been sterilized by filtration.
The TXN protein solution is provided at a concentration of 1 mg/ml in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
For short-term storage (up to 2-4 weeks), the product should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein such as HSA or BSA (0.1%) is advised for long-term storage to maintain protein stability. To avoid protein degradation, it is crucial to minimize freeze-thaw cycles.
The purity of the TXN protein is determined to be greater than 90% based on SDS-PAGE analysis.
The specific activity of TXN is assessed by measuring its ability to reduce insulin, resulting in increased insulin precipitation and a corresponding rise in absorbance at 650 nm. The specific activity is determined to be greater than 60 A650/cm/min/mg.
TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MGSMVKLIES KEAFQEALAA AGDKLVVVDF SATWCGPCKM IKPFFHSLCD KYSNVVFLEV DVDDCQDVAA DCEVKCMPTF QFYKKGQKVG EFSGANKEKL EASITEYA.
Product Science Overview
Thioredoxin (TRX or TXN) is a class of small redox proteins present in all organisms, playing a crucial role in various biological processes, including redox signaling . Thioredoxin from mouse recombinant sources is often used in research to study its functions and applications in mammalian systems.
Thioredoxin is a 12-kilodalton oxidoreductase protein characterized by a conserved active site with a CXXC motif, where two cysteine residues are key to its ability to reduce other proteins . The primary function of thioredoxin is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds . This protein is maintained in its reduced state by the flavoenzyme thioredoxin reductase in a NADPH-dependent reaction .
Thioredoxins are essential for life in mammals and are involved in many critical cellular functions. They act as electron donors to peroxidases and ribonucleotide reductase, playing a significant role in maintaining cellular redox balance . Disruption of this balance can lead to cell death, highlighting the importance of thioredoxin in cellular health .
Recombinant thioredoxin from mouse sources is typically prepared using bacterial expression systems. The gene encoding mouse thioredoxin is cloned into an expression vector, which is then introduced into a bacterial host such as Escherichia coli. The bacteria are cultured, and the thioredoxin protein is expressed, harvested, and purified using techniques such as affinity chromatography.
Mouse recombinant thioredoxin is widely used in research to study its role in redox signaling, oxidative stress response, and various cellular processes. It is also used to investigate the therapeutic potential of thioredoxin in diseases related to oxidative stress and inflammation.
