NDUFB4 Human

NADH Dehydrogenase 1 Beta Subcomplex 4 Human Recombinant

This product consists of the human NDUFB4 protein, recombinantly produced in E. coli. It is a single polypeptide chain of 110 amino acids (including a 23 amino acid His-tag at the N-terminus for purification) with a molecular weight of 12.6 kDa. The protein is not glycosylated. It has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13039
Source
E.Coli
Appearance
A clear, colorless solution that has been sterilized by filtration.

NDUFB9 Human

NADH Dehydrogenase 1 Beta Subcomplex 9 Human Recombinant

Recombinant human NDUFB9, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 202 amino acids (1-179) with a molecular weight of 24.2 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13142
Source
Escherichia Coli.
Appearance
A clear, sterile solution that has been filtered.

NQO2 Human

NAD(P)H Dehydrogenase Quinone 2 Human Recombinant

Recombinant human NQO2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 251 amino acids (specifically, amino acids 1 to 231) and possessing a molecular weight of 28.1 kDa. This protein is engineered with a 20 amino acid His-Tag fused to its N-terminus to facilitate purification through standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13949
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

PDHX Human

Pyruvate Dehydrogenase Complex, Component X Human Recombinant

Recombinant PDHX Human is a single, non-glycosylated polypeptide chain produced in E. coli. It comprises 471 amino acids (54-501 a.a), has a molecular weight of 50.4 kDa, and includes a 23 amino acid His-tag fused to the N-terminus. Proprietary chromatographic techniques are used to purify PDHX.
Shipped with Ice Packs
Cat. No.
BT14020
Source
Escherichia Coli.
Appearance
A clear solution that has been sterile filtered.

PGD Human

Phosphogluconate Dehydrogenase Human Recombinant

Recombinant human 6PGD, expressed in E. coli, is a non-glycosylated polypeptide chain containing 503 amino acids (with amino acids 1-483 present) and having a molecular mass of 55.3 kDa. The protein includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14117
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

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 has a molecular weight of 55.3 kDa.
PGD Human is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT14197
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless solution.

RDH12 Human

Retinol Dehydrogenase 12 Human Recombinant

Recombinant human RDH12, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 303 amino acids (residues 39-316) with a molecular weight of 33.5 kDa. This protein is expressed with a 25 amino acid His-tag fused to the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14268
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ACADVL Human

Acyl-CoA Dehydrogenase, Very Long Chain Human Recombinant

Recombinant human ACADVL, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 636 amino acids (residues 41-655). With a molecular weight of 68.5 kDa, it includes a 21 amino acid His-Tag at the N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6547
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

ADH1A Human

Alcohol Dehydrogenase 1A Human Recombinant

This recombinant ADH1A protein is produced in E. coli and lacks glycosylation. It consists of 375 amino acids (residues 1-375) and has a molecular weight of 42kDa. A 20 amino acid His-tag is fused to the N-terminus to facilitate purification. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6641
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

ACADM Human

Acyl-Coenzyme A Dehydrogenase, C-4 to C-12 Human Recombinant

Recombinant Human ACADM, produced in E. coli, is a single polypeptide chain without any sugar molecules attached (non-glycosylated). It consists of 417 amino acids (specifically amino acids 26 to 421) and has a molecular weight of 45.9 kDa. For purification and further applications, a 21 amino acid His-Tag is attached to the N-terminus of the ACADM protein.
Shipped with Ice Packs
Cat. No.
BT6344
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by 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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