ADH5 Human

Alcohol Dehydrogenase 5 Human Recombinant

Recombinant ADH5, expressed in E. coli, is a single polypeptide chain consisting of 398 amino acids (1-374) with a molecular weight of 42.3 kDa. This protein is fused to a 24 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6956
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

ADH6 Human

Alcohol Dehydrogenase 6 Human Recombinant

Recombinant human ADH6, produced in E. coli, is a single polypeptide chain consisting of 399 amino acids (residues 1-375) with a molecular weight of 42.4 kDa. This protein includes a 24 amino acid His-tag fused at the N-terminus and is purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7063
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

ALDH1A1 Human

Aldehyde Dehydrogenase 1A1 Human Recombinant

Recombinant human ALDH1A1 is a single, non-glycosylated polypeptide chain produced in E. coli. It has a molecular weight of 54.8 kDa, containing 501 amino acids (1-501).
Shipped with Ice Packs
Cat. No.
BT7140
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

ALDH1A1 Human, Active

Aldehyde Dehydrogenase 1A1 Human Recombinant, Active

ALDH1A1 Human recombinant protein is a single, non-glycosylated polypeptide chain with a molecular weight of 54.8 kDa. It is produced in E. coli and consists of 501 amino acids (1-501 a.a.).
Shipped with Ice Packs
Cat. No.
BT7196
Source
Escherichia Coli.
Appearance
The protein solution appears as a clear, sterile-filtered solution.

ALDH2 Human

Aldehyde Dehydrogenase-2 Human Recombinant

Recombinantly produced in E.Coli, ALDH2 Human Recombinant is a single, non-glycosylated polypeptide chain comprising 501 amino acids (18-517 a.a.). With a molecular mass of 54.5 kDa, the ALDH2 protein undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7265
Source
Escherichia Coli.
Appearance
The product appears as a clear solution that has undergone sterile filtration.

GAPDH Human, Active

Glyceraldehyde-3-Phosphate Dehydrogenase Human Recombinant, Active

This product consists of the active human GAPDH enzyme, recombinantly produced in E. coli. It is a single polypeptide chain with 335 amino acids (1-335), resulting in a molecular weight of 36kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8517
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GAPDH Mouse

GAPDH Mouse Recombinant

This product consists of recombinant mouse GAPDH protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 356 amino acids (amino acids 1-333) and has a molecular mass of 38.2 kDa. A 23 amino acid His-tag is fused to the N-terminus of the protein to facilitate purification, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8595
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GAPDH Mouse, Active

GAPDH Mouse Recombinant, Active

This product consists of the recombinant form of mouse GAPDH, expressed in E. coli. It is a single, non-glycosylated polypeptide chain composed of 356 amino acids (residues 1-333), resulting in a molecular weight of 38.2 kDa. A 23 amino acid His-tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8654
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

GCDH Human

Glutaryl-Coenzyme A Dehydrogenase Human Recombinant

Recombinant human GCDH, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 415 amino acids (specifically, residues 45-438). It has a molecular weight of 45.8 kDa. A 21-amino acid His-Tag is fused to the N-terminus of the GCDH protein. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8747
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HADH Human

Hydroxyacyl-Coenzyme A Dehydrogenase Human Recombinant

Recombinant human HADH is expressed in E. coli. A 21 amino acid His tag is fused to the N-terminus of the protein. The purified, non-glycosylated, monomeric protein migrates as a single band with an apparent molecular mass of 35.1 kDa by SDS-PAGE. The protein contains 323 amino acids, with amino acids 13-314 corresponding to HADH.
Shipped with Ice Packs
Cat. No.
BT9489
Source
Escherichia Coli.
Appearance
The product is a clear, colorless, and sterile-filtered 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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