Enzymes
Product List
SPR Human
Sepiapterin Reductase Human Recombinant
Sepiapterin Reductase is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
SPR Mouse
Sepiapterin Reductase Mouse Recombinant
SPR Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262 a.a) and having a molecular mass of 30.3kDa.
SPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
TP53I3 Human
Tumor Protein p53 Inducible Protein 3 Human Recombinant
TP53I3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 352 amino acids (1-332 a.a.) and having a molecular mass of 37.6 kDa. TP53I3 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
TRXR E.Coli
Thioredoxin Reductase E.Coli Recombinant
TrxR Yeast
Thioredoxin Reductase (NADPH) Yeast Recombinant
Thioredoxin Reductase is purified by proprietary chromatographic techniques.
TXNRD1 Human
Thioredoxin Reductase 1 Human Recombinant
TXNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated,
polypeptide chain containing 508 amino acids (161-647 a.a.) and having a molecular mass of 55.7 kDa. TXNRD1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.
TXNRD1 Human 161-649 a.a.
Thioredoxin Reductase 1 161-649 a.a. Human Recombinant
TXNRD3NB Human
Thioredoxin Reductase 3 Neighbor Human Recombinant
WWOX Human
WW Domain Containing Oxidoreductase Human Recombinant
The WWOX is purified by proprietary chromatographic techniques.
AKR1A1 Human
Aldo-Keto Reductase Family 1 Member A1 Human Recombinant
AKR1A1 is purified by proprietary chromatographic techniques.
Introduction
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 .
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 .
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 .
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 .
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 .
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 .
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.
