TXN1 Human, His

Thioredoxin Human Recombinant, His Tag
Cat. No.
BT12306
Source
Escherichia Coli.
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

Product Specs

Introduction
Thioredoxins are a class of small redox proteins found across all life forms, characterized by the presence of a conserved Cys-Gly-Pro-Cys active site containing a disulfide bridge. These proteins play a crucial role in cellular redox regulation by facilitating the reduction of disulfide bonds in other proteins. Thioredoxin's activity centers around the reversible oxidation of its two cysteine residues, which enables it to donate electrons and protons, thereby converting disulfide bonds to dithiols in target proteins. This process is vital for various cellular functions, including DNA synthesis, protein folding, and the regulation of transcription factors associated with cell growth and death.
Description
Recombinant Human Thioredoxin, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 125 amino acids. The protein consists of the native sequence for human thioredoxin (105 amino acids) with an additional 20 amino acid His-tag fused at the N-terminus to facilitate purification. The molecular weight of the recombinant protein is approximately 13.9 kDa, though it may appear larger on SDS-PAGE due to the His-tag. The protein has been purified using standard chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The TXN1 protein is supplied in a solution of 1x phosphate-buffered saline (PBS) at pH 7.4.
Stability
For short-term storage (up to four weeks), the solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein like bovine serum albumin (BSA) or human serum albumin (HSA) to a final concentration of 0.1% is advised for long-term storage. Repeated freezing and thawing of the solution should be avoided.
Biological Activity
The biological activity of the recombinant TXN1 protein is determined by measuring its ability to reduce insulin, resulting in increased insulin precipitation. The specific activity is measured as the change in absorbance at 650 nm per minute per mg of protein and falls within the range of 7-10 A650/min/mg.
Purity
The purity of the TXN1 protein is greater than 95% as assessed by SDS-PAGE analysis.
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.

Product Science Overview

Introduction

Thioredoxin (TRX) is a small redox protein that plays a crucial role in many biological processes, including redox signaling and the reduction of oxidized cysteine residues. In humans, thioredoxin is encoded by the TXN gene and is essential for life. The recombinant form of thioredoxin, tagged with a histidine (His) tag, is commonly used in research and biotechnology for its ease of purification and functional versatility.

Structure and Function

Thioredoxin is a 12-kDa protein that contains a characteristic thioredoxin fold and an active site with a dithiol motif (CXXC). This motif is critical for its ability to reduce other proteins by cleaving disulfide bonds. The His tag, typically added to the N-terminus of the protein, facilitates purification through affinity chromatography techniques .

The primary function of thioredoxin is to act as an electron donor to peroxidases and ribonucleotide reductase, among other substrates. It is maintained in its reduced state by thioredoxin reductase in a NADPH-dependent reaction . Thioredoxin is involved in various cellular processes, including DNA synthesis, defense against oxidative stress, and regulation of transcription factors .

Recombinant Thioredoxin Production

Recombinant human thioredoxin with a His tag is produced in Escherichia coli (E. coli) expression systems. The His tag allows for efficient purification using nickel-affinity chromatography. The recombinant protein is typically purified to a high degree of purity (>95%) and is available in a liquid form, stored in phosphate-buffered saline (PBS) at pH 7.4 .

Applications

Recombinant thioredoxin is widely used in biochemical and biophysical studies due to its stability and functional properties. It is employed in assays to measure redox activity, protein-protein interactions, and as a fusion partner to enhance the solubility of other recombinant proteins .

Biological Significance

Thioredoxin is essential for cellular redox homeostasis and has been implicated in various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders. Its ability to modulate the redox state of cells makes it a potential therapeutic target .

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