DsbA

Disulfide Oxidoreductase Recombinant

Disulfide Oxidoreductase, a periplasmic protein derived from E. coli, is produced through expression in E. coli. It consists of 208 amino acids and has a molecular weight of 23,149 Daltons. The purification of DsbA is achieved using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18628
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

AKR7A3 Human, His

Aldo-Keto Reductase Family 7 Member A3 Human Recombinant, His Tag

Recombinant human AKR7A3, expressed in E. coli, is a single-chain polypeptide with a His tag (39 amino acids) at the N-terminus. It is non-glycosylated and consists of 370 amino acids (residues 1-331), resulting in a molecular weight of 41.6 kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16996
Source
Escherichia Coli.
Appearance
The solution is clear, colorless, and sterile-filtered.

AKR7A3, Human

Aldo-Keto Reductase Family 7 Member A3 Human Recombinant

Recombinant human AKR7A3 produced in E. coli is a single, non-glycosylated polypeptide chain consisting of 331 amino acids (1-331) with a molecular weight of 37.7 kDa. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17087
Source

Escherichia Coli.

Appearance
Clear, colorless solution, sterile-filtered.

BLVRA Human

Biliverdin Reductase A Human Recombinant

Recombinant human BLVRA, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 295 amino acids, with amino acids 3 to 296 from the original sequence and an additional Methionine at the N-terminus. The protein has a molecular mass of 33.3 kDa. Note that the molecular weight observed on SDS-PAGE might be slightly higher. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17172
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CBR1 Human

Carbonyl Reductase-1 Human Recombinant

Recombinant Human CBR1, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 277 amino acids (residues 1-277). With a molecular weight of 30 kDa, it is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17431
Source
Escherichia Coli.
Appearance
A clear, sterile solution devoid of color.

CBR3 Human

Carbonyl Reductase-3 Human Recombinant

This product consists of recombinant human CBR3, expressed in E. coli, with an N-terminal His-tag. The protein is a single, non-glycosylated polypeptide chain comprising 297 amino acids (including a 20 amino acid His-tag; tag sequence not provided) with a molecular weight of 33 kDa. The protein has been purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17555
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

CBR4 Human

Carbonyl Reductase-4 Human Recombinant

CBR4 Human Recombinant, encompassing amino acids 1-237, is produced in E. coli with an N-terminal 20 amino acid His tag. This non-glycosylated polypeptide chain comprises 257 amino acids, resulting in a molecular weight of 27.5 kDa. Purification of CBR4 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17649
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

CRYZL1 Human

Quinone Oxidoreductase-like Protein 1 Human Recombinant

Recombinant CRYZL1, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 369 amino acids, specifically spanning from amino acid positions 1 to 349. With a molecular weight of 40.8 kDa, the protein features a 20 amino acid His Tag fused at its N-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17719
Source
Escherichia Coli.
Appearance
The product appears as a colorless solution that has been sterilized through filtration.

CYB5R1 Human

Cytochrome B5 Reductase 1 Human Recombinant

Recombinant human CYB5R1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 300 amino acids (residues 29-305). It has a molecular weight of 33.8 kDa. The protein includes a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17797
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

CYB5R2 Human

Cytochrome B5 Reductase 2 Human Recombinant

Recombinant CYB5R2, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 299 amino acids (specifically, amino acids 1 to 276) and possessing a molecular weight of 33.8 kDa. The CYB5R2 protein is fused to a 23 amino acid His-tag at its N-terminus.
Shipped with Ice Packs
Cat. No.
BT17852
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.
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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