Thioredoxin: A Versatile Protein for Redox Regulation

REF #: 3199485
Short description
  • Thioredoxin: A 12 kDa ubiquitous protein that mediates the reduction of disulfide bonds in proteins.
  • Purity: 90% (SDS-PAGE)
  • Tag: N-terminal histidine tagged
  • Main Activity: At least 5 units/mg
  • Form: Lyophilized powder
  • CAS Number: 52500-60-4
  • Expression System: E. coli
  • Tool for: Studying redox regulation in various biological systems
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  • Procurenet Team Tshim Sha Tsui
    Hong Kong Hong Kong 3 years
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Thioredoxin: A Versatile Protein for Redox Regulation

The Thioredoxin protein is an indispensable tool for researchers studying redox regulation and disulfide bond reduction. Its ubiquity in various biological systems highlights its importance in understanding cellular functions and molecular processes.

Key Features:

  • 12 kDa Thioredoxin protein
  • Mediates the reduction of disulfide bonds in proteins
  • High purity of 90% (SDS-PAGE)
  • N-terminal histidine tagged
  • Essentially salt-free
  • Recombinant protein expressed in E. coli
  • Main activity of at least 5 units/mg
  • Supplied as a lyophilized powder
  • CAS number: 52500-60-4

Understanding Redox Regulation and Disulfide Bond Reduction

When studying redox regulation, Thioredoxin enables the investigation of protein folding, structural stability, and functional activity. It plays a vital role in maintaining the redox homeostasis by catalyzing the reduction of disulfide bonds in proteins. These disulfide bonds are critical for protein structure and function, and their reversible reduction is crucial in cellular processes such as DNA synthesis, cell signaling, and protection against oxidative stress.

Purity and Detection

The Thioredoxin supplied is of the highest quality, with a purity of 90% determined by SDS-PAGE. This level of purity ensures minimal contamination and reliable results in experiments. Its N-terminal histidine tag facilitates easy detection, purification, and downstream applications.

Salt-Free Composition

The Thioredoxin is essentially salt-free, eliminating potential interference with downstream applications, such as enzymatic assays or structural studies. This makes it an ideal choice for researchers who require a salt-free protein source. The absence of salts simplifies protein purification and reduces the risk of protein aggregation or precipitation.

Recombinant Expression and Reliability

As a recombinant protein expressed in E. coli, the Thioredoxin provides consistent and reproducible results across experiments. Its expression in E. coli allows for high protein yields, making it readily available for various research applications. The purity, activity, and stability of the Thioredoxin protein are rigorously tested to ensure its suitability for a wide range of studies.

Lyophilized Powder Formulation

The Thioredoxin is supplied in a lyophilized powder form, which provides long-term stability and ease of handling. This formulation allows for convenient storage and transport, minimizing the risk of degradation. To reconstitute the protein, simply dissolve the lyophilized powder in a suitable buffer at the desired concentration.

Unleash the Potential with Thioredoxin

In summary, Thioredoxin is an essential protein for researchers investigating redox regulation and disulfide bond reduction. Its high purity, N-terminal histidine tag, salt-free composition, and recombinant expression in E. coli make it a reliable tool for studying various biological systems. Whether unraveling protein folding mechanisms, deciphering cellular signaling pathways, or developing new therapeutic approaches, Thioredoxin offers researchers the confidence to pursue groundbreaking discoveries.

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