TrxR Yeast

Thioredoxin Reductase (NADPH) Yeast Recombinant

Thioredoxin Reductase (NADPH) Yeast Recombinant is produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21082
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

TXNRD1 Human

Thioredoxin Reductase 1 Human Recombinant

Recombinant human TXNRD1, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 55.7 kDa. It encompasses amino acids 161-647 of the TXNRD1 protein and includes a 21-amino acid His tag at the N-terminus. The protein is purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21171
Source
Escherichia Coli.
Appearance
A clear, colorless solution, sterile-filtered.

TXNRD1 Human 161-649 a.a.

Thioredoxin Reductase 1 161-649 a.a. Human Recombinant

Recombinant human TXNRD1, spanning amino acids 161 to 649, is expressed in E. coli with an N-terminal 21-amino acid His tag. This non-glycosylated polypeptide chain consists of 510 amino acids, resulting in a molecular weight of 55.9 kDa. The protein undergoes purification using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT21242
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution without any visible color.

TXNRD3NB Human

Thioredoxin Reductase 3 Neighbor Human Recombinant

Recombinant human TXNRD3NB, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-133 a.a) and has a molecular mass of 16.7 kDa. TXNRD3NB is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21350
Source
Escherichia Coli.
Appearance
Sterile filtered, clear solution.

WWOX Human

WW Domain Containing Oxidoreductase Human Recombinant

Recombinant human WWOX protein is produced in E. coli with a 20 amino acid His tag at the N-terminus. This non-glycosylated polypeptide chain consists of 254 amino acids (1-234 a.a.) and has a molecular weight of 28.3 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21426
Source
Escherichia Coli.
Appearance
A clear, colorless, and sterile filtered solution.
Definition and Classification

Reductase is an enzyme that catalyzes the reduction of molecules by adding electrons, typically through the transfer of hydrogen atoms. These enzymes are part of the broader class of oxidoreductases, which facilitate redox reactions by transferring electrons between molecules. Reductases can act as both oxidases and reductases depending on the reaction conditions . They are classified under the EC number classification system as EC 1, with further subdivisions based on the specific type of reaction they catalyze .

Biological Properties

Reductases exhibit several key biological properties, including their ability to catalyze reduction reactions essential for various metabolic processes. They are expressed in different patterns across various tissues, with some being ubiquitous while others are tissue-specific. For instance, ribonucleotide reductase is crucial for DNA synthesis and is found in all proliferating cells . The tissue distribution of reductases can vary, with some being highly expressed in the liver, where detoxification processes are prominent .

Biological Functions

The primary biological functions of reductases include facilitating metabolic reactions, such as the synthesis of DNA, RNA, and proteins. They play a critical role in immune responses by participating in the reduction of reactive oxygen species, thus protecting cells from oxidative stress . Reductases are also involved in pathogen recognition and the subsequent immune response, as they help maintain the redox balance within cells .

Modes of Action

Reductases interact with other molecules and cells through various mechanisms. They often bind to specific substrates and cofactors, such as NADH or NADPH, to facilitate electron transfer. This binding initiates downstream signaling cascades that regulate cellular processes like metabolism and cell division . For example, ribonucleotide reductase catalyzes the reduction of ribonucleotides to deoxyribonucleotides, a critical step in DNA synthesis .

Regulatory Mechanisms

The expression and activity of reductases are tightly regulated through multiple mechanisms. Transcriptional regulation involves the activation or repression of genes encoding reductases in response to cellular signals. Post-translational modifications, such as phosphorylation and acetylation, can alter the enzyme’s activity, stability, and interaction with other proteins . Additionally, allosteric regulation allows reductases to respond to changes in the cellular environment by altering their conformation and activity .

Applications

Reductases have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. In research, they are used to study metabolic pathways and disease mechanisms. Diagnostic tools often utilize reductases to detect specific biomolecules or changes in redox states. Therapeutically, reductase inhibitors are employed to treat conditions like cancer and cardiovascular diseases by targeting specific metabolic pathways .

Role in the Life Cycle

Throughout the life cycle, reductases play vital roles from development to aging and disease. During development, they are essential for DNA synthesis and cell proliferation. In adulthood, they help maintain cellular homeostasis and protect against oxidative damage. As organisms age, the activity of reductases can decline, leading to increased susceptibility to diseases such as cancer and neurodegenerative disorders .

Reductases are indispensable enzymes with diverse roles in biological processes, making them crucial targets for research and therapeutic interventions.

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