Enzymes
Product List
NDUFA4 Human
NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant
NDUFA5 Human
NADH Dehydrogenase 1 Alpha Subcomplex 5 Human Recombinant
NDUFA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFAF1 Human
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant
NDUFAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFAF2 Human
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant
NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.
NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFAF4 Human
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 4 Human Recombinant
NDUFAF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFB4 Human
NADH Dehydrogenase 1 Beta Subcomplex 4 Human Recombinant
NDUFB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFB9 Human
NADH Dehydrogenase 1 Beta Subcomplex 9 Human Recombinant
NDUFB9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFS2 Human
Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant
NDUFS3 Human
Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant
NDUFS4 Human
Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant
The NDUFS4 is purified by proprietary chromatographic techniques.
Introduction
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 .
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 .
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 .
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 .
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 .
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 .
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 .
