GMPR2 Human

Guanosine Monophosphate Reductase 2 Human Recombinant

GMPR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40 kDa.
GMPR2 is fused to a 20 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18864
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GOR E.Coli

Glutathione Oxidoreductase E.Coli Recombinant

GOR E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 51.2kDa.
GOR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18943
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GRHPR Human

Glyoxylate Reductase/Hydroxypyruvate Reductase Human Recombinant

GRHPR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a.) and having a molecular mass of 37.8 kDa. The GRHPR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19034
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GSR Human

Glutathione Reductase Human Recombinant

GSR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 504 amino acids (43-522) and having a molecular mass of 54.3kDa.
GSR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19111
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

KDSR Human

3-Ketodihydrosphingosine Reductase Human Recombinant

KDSR Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids (26-270 a.a.) and having a molecular mass of 29kDa. The KDSR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19206
Source
Escherichia Coli.
Appearance
The KDSR is supplied as a sterile filtered colorless solution.

MECR Human

Mitochondrial Trans-2-Enoyl-CoA Reductase Human Recombinant

MECR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (54-373 a.a.) and having a molecular mass of 49.8 kDa. The MECR is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19306
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

MSRA E.Coli

Methionine Sulfoxide Reductase A E.Coli Recombinant

MSRA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a.) and having a molecular mass of 25.4kDa.
MSRA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19373
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

MSRA Human

Methionine Sulfoxide Reductase A Human Recombinant

MSRA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (24-235) and having a molecular mass of 26.2kDa.
The MSRA is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19453
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

MSRB E.Coli

Methionine Sulfoxide Reductase B E.Coli Recombinant

MSRB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids (1-137 a.a.) and having a molecular mass of 17.6kDa.
MSRB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19524
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

MSRB2 Human

Methionine Sulfoxide Reductase B2 Human Recombinant

MSRB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (21-182a.a.) and having a molecular mass of 19.5kDa.
MSRB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19607
Source
Escherichia Coli.
Appearance
Sterile Filtered clear 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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