Enzymes
Product List
NDUFS5 Human
Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant
NDUFS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFS6 Human
Histidine NADH Dehydrogenase Fe-S Protein 6 Human Recombinant
NDUFV2 Human
NADH Dehydrogenase Flavoprotein 2 Human Recombinant
NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NDUFV3 Human
NADH Dehydrogenase Flavoprotein 3 Human Recombinant
NDUFV3 is fused to a 23 amino acid His-
tag at N-terminus & purified by proprietary chromatographic techniques.
NQO1 Human
NAD(P)H Dehydrogenase Quinone 1 Human Recombinant
The NQO1 is purified by proprietary chromatographic techniques.
NQO1 Human, Active
NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant
NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa.
NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
NQO2 Human
NAD(P)H Dehydrogenase Quinone 2 Human Recombinant
PDHX Human
Pyruvate Dehydrogenase Complex, Component X Human Recombinant
PGD Human
Phosphogluconate Dehydrogenase Human Recombinant
PGD Human, Active
Phosphogluconate Dehydrogenase, Active Human Recombinant
PGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and having a molecular mass of 55.3 kDa.
PGD Human is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Escherichia Coli.
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 .
