NDUFS2 Human

Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant

Recombinant human NDUFS2, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 410 amino acids (77-463a.a) with a molecular mass of 46.5kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13248
Source
Escherichia Coli.
Appearance
The product appears as a clear, sterile-filtered solution.

NDUFS3 Human

Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant

Recombinant Human NDUFS3, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 249 amino acids (residues 37-264) with a molecular weight of 28.7 kDa. A 21 amino acid His-tag is fused to the N-terminus of NDUFS3. The protein is purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13335
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

NDUFS4 Human

Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant

Recombinant NDUFS4 Human, produced in E.Coli, is a single, non-glycosylated polypeptide chain consisting of 134 amino acids (43-175 a.a.). It has a molecular weight of 15.5 kDa. The purification of NDUFS4 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13397
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution, free from particulate matter.

NDUFS5 Human

Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant

Recombinant Human NDUFS5, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 129 amino acids (1-106a.a), including a 23 amino acid His-tag fused at the N-terminus, and has a molecular mass of 14.9 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13450
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

NDUFS6 Human

Histidine NADH Dehydrogenase Fe-S Protein 6 Human Recombinant

This product encompasses various synonyms for NADH Dehydrogenase Fe-S Protein 6, including NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa, NADH-Coenzyme Q Reductase, Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, and CI13KDA.
Shipped with Ice Packs
Cat. No.
BT13532
Source
Escherichia Coli.
Appearance
The product appears as a clear solution that has undergone sterile filtration.
Definition and Classification

Dehydrogenases are enzymes belonging to the oxidoreductase class, which catalyze the removal of hydrogen atoms from a substrate, transferring them to an electron acceptor such as NAD+, NADP+, FAD, or FMN . These enzymes play a crucial role in oxidation-reduction reactions within cells. Dehydrogenases are classified based on the type of substrate they act upon, such as alcohol dehydrogenase, lactate dehydrogenase, and glyceraldehyde-3-phosphate dehydrogenase .

Biological Properties

Dehydrogenases exhibit key biological properties, including their ability to regulate cellular redox balance by maintaining the ratio of NADH to NAD+ . They are expressed in various tissues and have distinct expression patterns. For instance, lactate dehydrogenase is found in the heart, liver, and muscles, while alcohol dehydrogenase is primarily located in the liver . These enzymes are crucial for cellular respiration and energy production .

Biological Functions

The primary biological function of dehydrogenases is to facilitate oxidation-reduction reactions, which are essential for cellular metabolism . They play a significant role in energy production by participating in pathways such as glycolysis, the citric acid cycle, and the electron transport chain . Dehydrogenases also contribute to immune responses and pathogen recognition by modulating the redox state of cells, which can influence signaling pathways involved in immune activation .

Modes of Action

Dehydrogenases operate by transferring hydrogen atoms from a substrate to an electron acceptor . This process involves binding to specific substrates and electron acceptors, forming enzyme-substrate complexes. For example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde with the help of NAD+ . The downstream signaling cascades triggered by dehydrogenase activity can lead to various cellular responses, including changes in gene expression and metabolic adjustments .

Regulatory Mechanisms

The expression and activity of dehydrogenases are tightly regulated through multiple mechanisms. Transcriptional regulation involves the control of gene expression by transcription factors that respond to cellular signals . Post-translational modifications, such as phosphorylation and acetylation, can alter the activity and stability of dehydrogenases . Additionally, allosteric regulation and feedback inhibition by metabolic intermediates play a role in modulating enzyme activity .

Applications

Dehydrogenases have numerous applications in biomedical research, diagnostics, and therapeutics. They are used as biomarkers for various diseases, such as lactate dehydrogenase in myocardial infarction . In research, dehydrogenases are employed to study metabolic pathways and enzyme kinetics . Therapeutically, they are targeted in drug development for conditions like cancer and metabolic disorders .

Role in the Life Cycle

Throughout the life cycle, dehydrogenases are involved in critical processes from development to aging and disease . During development, they support rapid cell growth and differentiation by providing energy and metabolic intermediates . In aging, changes in dehydrogenase activity can affect cellular metabolism and contribute to age-related diseases . In diseases such as Alzheimer’s and Parkinson’s, altered dehydrogenase function is linked to pathogenesis and progression .

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