Enzymes
Product List
AKR1C3 Human
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant
Recombinant human AKR1C3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 323 amino acids (1-323) with a molecular weight of 36.8 kDa.
The protein undergoes purification using proprietary chromatographic methods.
Escherichia Coli.
AKR1C3 Human, His
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag
AKR1C4 Human
Aldo-Keto Reductase Family 1 Member C4 Human Recombinant
Recombinant human AKR1C4, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 323 amino acids (1-323aa). It has a molecular weight of 37kDa.
AKR1A1 Human
Aldo-Keto Reductase Family 1 Member A1 Human Recombinant
AKR1B1 Human
Aldose Reductase Human Recombinant
AKR1B1 Mouse
Aldose Reductase Mouse Recombinant
AKR1B10 Human
Aldo-Keto Reductase Family 1 Member B10 Human Recombinant
AKR1C1 Human
Aldo-Keto Reductase Family 1 Member C1 Human Recombinant
Recombinant human AKR1C1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 323 amino acids (residues 1-323). It has a molecular weight of 36.7 kDa.
The purification of AKR1C1 is achieved using proprietary chromatographic methods.
Escherichia Coli.
AKR1C1 Human, His
Aldo-Keto Reductase Family 1 Member C1 Human Recombinant, His Tag
BLVRB Human
Biliverdin Reductase B Human Recombinant
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.
