DCXR Human, Bioactive

Dicarbonyl/L-Xylulose Reductase Human Recombinant, Bioactive

DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18144
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

DECR1 Human

2,4-Dienoyl CoA Reductase 1 Human Recombinant

DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa.
The DECR1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18231
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DECR2 Human

2,4-Dienoyl CoA Reductase 2 Human Recombinant

DECR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 33.2kDa.
DECR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18302
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DHFR Human

Dihydrofolate Reductase Human Recombinant

DHFR Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.
The DHFR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18381
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DHFR Mouse

Dihydrofolate Reductase Mouse Recombinant

DHFR Mouse Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa. The DHFR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18461
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DHRS4 Human

Dehydrogenase/Reductase Member 4 Human Recombinant

DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.
DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18510
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DHRS9 Human

Dehydrogenase/Reductase Member 9 Human Recombinant

DHRS9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (18-319) and having a molecular mass of 35.9kDa.
DHRS9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18563
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DsbA

Disulfide Oxidoreductase Recombinant

Disulfide Oxidoreductase produced in E.Coli is a periplasmic protein isolated from E. coli, containing 208 amino acids having a molecular mass of 23,149 Dalton.
The DsbA is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18628
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

DsbA E.Coli

Disulfide Oxidoreductase E.Coli Recombinant

DsbA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (20-208) and having a molecular mass of 21.2 kDa. DsbA E.Coli is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18689
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

GMPR Human

Guanosine Monophosphate Reductase Human Recombinant

GMPR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 365 amino acids (1-345) and having a molecular mass of 39.5kDa.
GMPR is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18781
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless 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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