TRXR E.Coli

Thioredoxin Reductase E.Coli Recombinant
Cat. No.
BT21004
Source
Escherichia Coli.
Synonyms
TRXB, TRXR, Thioredoxin Reductase.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek'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.
Shipped with Ice Packs
In Stock

Description

TRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard chromatography.

Product Specs

Introduction
Thioredoxin reductase (TRXR) is a ubiquitous enzyme found in many organisms. It plays a crucial role in various cellular processes, including cell growth, regulation of p53 activity, and protection against oxidative stress. Mammalian TRXR is known to reduce thioredoxins as well as other substrates like selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxide.
Description
Recombinant TRXR from E. coli is produced in E. coli and is a single, non-glycosylated polypeptide chain. It consists of 321 amino acids (1-321 a.a.) and has a molecular weight of 34.6 kDa. The protein is purified using standard chromatography techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The TRXR E.Coli solution is supplied in a buffer containing 20mM Tris HCl at pH 8, 1mM DTT (dithiothreitol), and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage, it is recommended to store the product frozen at -20°C. To ensure stability during long-term storage, consider adding a carrier protein such as 0.1% HSA (human serum albumin) or BSA (bovine serum albumin). Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the TRXR protein is greater than 90% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured to be 4-5 units per ml. This is determined using a coupled assay involving DTNB (5,5'-dithiobis-(2-nitrobenzoic acid)) and NADPH. The amount of TNB (2-nitro-5-thiobenzoate) produced as a result of NADPH oxidation is measured by absorbance at 412 nm.
Synonyms
TRXB, TRXR, Thioredoxin Reductase.
Source
Escherichia Coli.
Amino Acid Sequence
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.

Product Science Overview

Importance of Thioredoxin Reductase

The thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is vital for maintaining a reducing environment in the cytoplasm. This system is involved in numerous cellular processes, such as DNA synthesis, repair, and defense against oxidative stress . The redox balance maintained by the thioredoxin system is crucial for cell viability and function.

Recombinant Expression in E. coli

E. coli is a widely used host for the production of recombinant proteins due to its well-established molecular tools, ease of cultivation, and ability to express high levels of heterologous proteins . The recombinant expression of thioredoxin reductase in E. coli allows for the production of large quantities of the enzyme, which can be purified and characterized for various applications.

Applications of Recombinant Thioredoxin Reductase

Recombinant thioredoxin reductase has several applications in biotechnology and research. It can be used in studies related to redox biology, oxidative stress, and cellular metabolism. Additionally, the enzyme is valuable in the development of therapeutic agents and vaccines, as it plays a role in maintaining cellular redox homeostasis .

Challenges and Advances

While the production of recombinant proteins in E. coli is generally straightforward, several challenges can arise, such as poor growth of the host, formation of inclusion bodies, and protein inactivity . Advances in molecular biology techniques have led to the development of various strategies to overcome these challenges, including the use of engineered strains, optimized expression vectors, and improved cultivation conditions .

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