BDH2 Human

3-Hydroxybutyrate Dehydrogenase, Type 2 Human Recombinant

Produced in E. coli, our BDH2 is a non-glycosylated, single polypeptide chain comprising 265 amino acids (1-245a.a.) with a molecular weight of 28.8 kDa. It features a 20 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7883
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

DHODH Human

Dihydroorotate Dehydrogenase Human Recombinant

This product consists of the recombinant human DHODH enzyme, produced in E. coli bacteria. It is a single polypeptide chain with a molecular weight of 42.3 kDa, encompassing amino acids 31 to 395. For purification purposes, a 25 amino acid His-tag is attached to the N-terminus. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7926
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DLD Human

Dihydrolipoamide Dehydrogenase Human Recombinant

This product consists of the recombinant human DLD protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 511 amino acids (residues 36-509) with a molecular weight of 54.4 kDa. The protein has a 37 amino acid Histidine tag fused at its N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7997
Source
Escherichia Coli.
Appearance
The product is supplied as a clear, colorless, and sterile filtered solution.

GAPDH Human

Glyceraldehyde-3-Phosphate Dehydrogenase Human Recombinant

Recombinant human GAPDH, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 335 amino acids, resulting in a molecular weight of 36 kDa. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT8219
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GLUD1 Human

Glutamate Dehydrogenase 1 Human Recombinant

Recombinant human GLUD1 protein expressed in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 528 amino acids (residues 54-558) with a molecular weight of 58.4 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT9155
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

GPD1 Human

Glycerol-3-Phosphate Dehydrogenase 1 Human Recombinant

Recombinant GPD1 from humans, produced in E. coli, is available as a single, non-glycosylated polypeptide chain. It comprises 349 amino acids (specifically, amino acids 1 to 349) and has a molecular weight of 37.5 kDa. The purification of GPD1 is achieved through standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9229
Source
Escherichia Coli.
Appearance
The product is a clear and colorless solution that has been sterilized by filtration.

GPD1L Human

Glycerol-3-Phosphate Dehydrogenase 1 Like Human Recombinant

Recombinant GPD1L Human, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 371 amino acids (specifically, amino acids 1 through 351). With a molecular weight of 40.6 kDa, this protein is fused to a 20 amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9330
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized through filtration.

GPD2 Human

Glycerol-3-Phosphate Dehydrogenase 2 Human Recombinant

Recombinant human GPD2, expressed in E. coli, is a non-glycosylated polypeptide chain containing a 558 amino acid fragment (residues 43-600). This fragment corresponds to the GlpA domain of the mature protein and has a molecular mass of 66.26 kDa, including a 4.5 kDa amino-terminal hexahistidine tag. GPD2 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9423
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

HPGD Human

Hydroxyprostaglandin Dehydrogenase 15-(NAD) Human Recombinant

This recombinant HPGD protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 286 amino acids (residues 1-266), with a molecular weight of 31.1 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.
BT9756
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

HPGD Mouse

Hydroxyprostaglandin Dehydrogenase 15-(NAD) Mouse Recombinant

Recombinant HPGD from Mouse, produced in E. coli, is a single polypeptide chain with a molecular weight of 31.6kDa. It consists of 292 amino acids, with the HPGD sequence spanning from amino acid 1 to 269. A 24 amino acid His-tag is fused to the N-terminus of the protein. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9842
Source

E.coli.

Appearance
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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