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Enzymes

Dehydrogenase

Creatine Kinases

Isomerase

Phosphatase

TPA

TGFBR

Transaminase

Cyclin-Dependent Kinase

PPARG

PI3-kinase

Transferase

Cyclin

Phosphorylase

Cyclophilin

Jun N-terminal Kinase

Jun Proto-Oncogene

Polymerase

Kallikrein

Protease

Deaminase

Ligase

Proteasome

Lipase

Decarboxylase

Lipocalin

Lyase

LYVE1

MMP

Protein Kinase-A

Protein Kinase-C

Protein Kinase Akt1/PKB alpha

Protein Kinases

TIMP

Mitogen-Activated Protein Kinase

Mutase

Natural Enzymes

Nuclease

Discoidin Domain Receptor Tyrosine Kinase

DNA Polymerase

TGM2

Reductase

EGF Receptor

Nucleotidase

Tyrosine Kinase

Endonuclease

Nudix Type Motif

Enolase

Ubiquitin Conjugating Enzyme

Enterokinase

Epimerase

Esterase

Oxidase

FGF Receptors

Oxygenase

FK506 Binding Protein

Uromodulin

VEGF Receptors

Fructosamine 3 Kinase

Paraoxonase

Galactosidase

Peptidase

Secreted Phospholipase A2

Glucosidase

Gluteradoxin

Other Enzymes

Serine Threonine Kinase

Glycogen synthase kinase

Sulfatase

Glycosylase

Synthase

Glyoxalase

Granzyme

ACE2

Guanylate Kinase

Hexokinase

Peroxiredoxin

Activating Transcription Factor

Histone Deacetylase

Adenylate Kinase

Heparanase

Protein Tyrosine Phosphatase

Hydratase

Synthetase

AHCY

Aldolase

Hydrolase

Alkaline Phosphatase

Asparaginase

Aurora Kinase

Beta Lactamase

Calcium/Calmodulin-Dependent Protein Kinase

TIE1,TIE2

Calcium and Integrin Binding

Carbonic Anhydrase

Hydroxylase

Casein Kinase

Cathepsin

Chitinase

Product List

UGDH Mouse

UDP-Glucose Dehydrogenase Mouse Recombinant

Recombinant UGDH Mouse, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 516 amino acids (specifically, amino acids 1 through 493), resulting in a molecular weight of 57.2 kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus and is purified using specialized chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT15203

Source

Escherichia Coli.

Appearance

A clear, sterile solution without any color.

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IDH1 Human

Isocitrate Dehydrogenase-1 Human Recombinant

This product consists of the human IDH1 enzyme, recombinantly produced in E. coli. This specific form is a single polypeptide chain that lacks glycosylation modifications and comprises 434 amino acids (with amino acids 1-414 representing the IDH1 sequence). Its molecular weight is approximately 48.8 kDa. For purification and detection purposes, a 20 amino acid His-tag is attached to the N-terminus.

Shipped with Ice Packs

Cat. No.

BT10333

Source

E.coli.

Appearance

Clear, colorless solution, sterilized by filtration.

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IDH3G Human

Isocitrate Dehydrogenase 3 (NAD+) Gamma Human Recombinant

Recombinant human IDH3G, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 375 amino acids (positions 40-393). It has a molecular weight of 41.1 kDa. A 21 amino acid His-tag is fused to the N-terminus of IDH3G. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT10399

Source

E.coli.

Appearance

A clear, colorless solution that has been sterilized by filtration.

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IMPDH1 Human

IMP Dehydrogenase 1 Human Recombinant

IMPDH1 Recombinant Human produced in E. coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514 a.a.) and having a molecular mass of 57.5 kDa. The IMPDH1 is fused to a 20 amino acid His-Tag at the N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT10438

Source

Escherichia Coli.

Appearance

Sterile filtered colorless solution.

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IMPDH2 Human

IMP Dehydrogenase 2 Human Recombinant

Recombinant Human IMPDH2, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 534 amino acids (residues 1-514). With a molecular mass of 58 kDa, it features a 20 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT10534

Source

E.coli.

Appearance

A clear, colorless solution, sterile-filtered.

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MDH2 Mouse

Malate Dehydrogenase 2 Mouse Recombinant

Recombinant MDH2 from mouse has been produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 335 amino acids (residues 25-338) with a molecular weight of 35.4 kDa. For purification purposes, a 21 amino acid His-tag is fused to the N-terminus. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT11802

Source

Escherichia Coli.

Appearance

Clear, colorless solution, sterile-filtered.

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MTHFD2 Human

MTHFD2 Human Recombinant

Recombinant human MTHFD2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 344 amino acids (residues 30-350), with a molecular weight of 37.2 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT11856

Source

Escherichia Coli.

Appearance

Clear, sterile solution after filtration.

View Details

NDUFA2 Human

NADH Dehydrogenase 1 Alpha Subcomplex 2 Human Recombinant

Recombinant human NDUFA2 protein expressed in E.coli. This protein is a single, non-glycosylated polypeptide chain consisting of 122 amino acids (residues 1-99) with a molecular weight of 13.3 kDa. It includes a 23 amino acid His-tag at the N-terminus. The protein has been purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT11927

Source

Escherichia Coli.

Appearance

Clear, colorless, and sterile filtered solution.

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NDUFA4 Human

NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant

This product is a recombinant human NDUFA4 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 104 amino acids (residues 1-81 of the native protein) with a molecular mass of 11.8 kDa. The 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.

BT11982

Source

E.coli.

Appearance

Clear, colorless, and sterile-filtered solution.

View Details

NDUFA5 Human

NADH Dehydrogenase 1 Alpha Subcomplex 5 Human Recombinant

Recombinant human NDUFA5, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 139 amino acids (residues 1-116). It has a molecular mass of 15.8 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT12043

Source

Escherichia Coli.

Appearance

Clear, colorless solution, sterile-filtered.

View Details

Showing 81 to 90 of 95 results

Introduction

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.