ADH5 Human

Alcohol Dehydrogenase 5 Human Recombinant

ADH5 Recombinant produced in E. coli is a single polypeptide chain containing 398 amino acids (1-374) and having a molecular mass of 42.3kDa.
ADH5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6956
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

ADH6 Human

Alcohol Dehydrogenase 6 Human Recombinant

ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.
ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7063
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

ALDH1A1 Human

Aldehyde Dehydrogenase 1A1 Human Recombinant

The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).
Shipped with Ice Packs
Cat. No.
BT7140
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ALDH1A1 Human, Active

Aldehyde Dehydrogenase 1A1 Human Recombinant, Active

The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).
Shipped with Ice Packs
Cat. No.
BT7196
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ALDH2 Human

Aldehyde Dehydrogenase-2 Human Recombinant

ALDH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 501 amino acids (18-517 a.a.) & having a molecular mass of 54.5 kDa.
The ALDH2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7265
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ALDH2 Mouse

Aldehyde Dehydrogenase 2 Mouse Recombinant

ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519 a.a) and having a molecular mass of 56.8kDa.
ALDH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7339
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ALDH2 Mouse, Active

Aldehyde Dehydrogenase 2 Mouse Recombinant, Active

ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519) and having a molecular mass of 56.8kDa.

ALDH2 Mouse is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7401
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ALDH3A1 Human

Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant

ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7475
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

ALDH5A1 Human

Aldehyde Dehydrogenase 5 A1 Human Recombinant

ALDH5A1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 509 amino acids (48-535 a.a.) and having a molecular mass of 54.6kDa. The ALDH5A1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7538
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ALDH6A1 Human

Aldehyde Dehydrogenase 6 A1 Human Recombinant

ALDH6A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (34-535 a.a) and having a molecular mass of 56.8kDa. ALDH6A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7631
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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