MSRB E.Coli

Methionine Sulfoxide Reductase B E.Coli Recombinant

Produced in E. coli, MSRB is a single, non-glycosylated polypeptide chain consisting of 157 amino acids (amino acids 1-137) with a molecular weight of 17.6kDa. This MSRB protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19524
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

MSRB2 Human

Methionine Sulfoxide Reductase B2 Human Recombinant

Recombinant MSRB2, expressed in E. coli, is a non-glycosylated polypeptide chain with a single chain. It consists of 183 amino acids, spanning from position 21 to 182, with an additional 21 amino acid His-tag fused at the N-terminus. The protein has a molecular weight of 19.5 kDa and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19607
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

MSRB3 Human

Methionine Sulfoxide Reductase B3 Human Recombinant

Recombinant human MSRB3, with an 8 amino acid His tag fused at the C-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 174 amino acids (21-185 a.a.) and has a molecular mass of 19 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19688
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NFNB E.Coli

Dihydropteridine Reductase E.Coli Recombinant

Recombinant NFNB, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 237 amino acids. This includes 217 amino acids of the NFNB protein (1-217 a.a.) and a 20 amino acid His-Tag fused at the N-terminus. With a molecular weight of 26 kDa, the protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19747
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PECR Human

Peroxisomal Trans-2-enoyl-CoA Reductase Human Recombinant

Recombinant human PECR, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 327 amino acids (residues 1-303) and possesses a molecular weight of 35.1 kDa. A 24 amino acid His-tag is fused to the N-terminus of PECR. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19843
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

PTGR1 Human

Prostaglandin Reductase 1 Human Recombinant

Recombinant human PTGR1, produced in E. coli, is a single polypeptide chain containing 354 amino acids (residues 1-329) with a molecular mass of 38.6 kDa. This protein includes a 25 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19930
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PTGR2 Human

Prostaglandin Reductase 2 Human Recombinant

Recombinant human PTGR2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 375 amino acids (residues 1-351) with a molecular weight of 41.1 kDa. A 24-amino acid His-tag is fused to the N-terminus of PTGR2. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19976
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

PYCR1 Human

Pyrroline-5-Carboxylate Reductase 1 Human Recombinant

Recombinant PYCR1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 339 amino acids (residues 1-319) with a molecular weight of 35.5 kDa. This protein contains a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20051
Source
Escherichia Coli.
Appearance
Clear, sterile filtered solution.

PYCR2 Human

Pyrroline-5-Carboxylate Reductase 2 Human Recombinant

This product consists of the recombinant human PYCR2 protein, expressed in E. coli and purified to a high degree. It is a single, non-glycosylated polypeptide chain with 343 amino acids (residues 1-320) and a molecular weight of 36 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus.
Shipped with Ice Packs
Cat. No.
BT20183
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterile-filtered.

PYCRL Human

Pyrroline-5-Carboxylate Reductase Like Human Recombinant

Recombinant human PYCRL, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 297 amino acids (1-274) and has a molecular weight of 31 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20259
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered 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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