LDHB Mouse

Lactate Dehydrogenase B Mouse Recombinant

This product is a recombinant LDHB protein derived from mice. It is produced in E. coli and purified to a high degree. The protein is a single, non-glycosylated polypeptide chain that contains 357 amino acids. It has a molecular mass of 39 kDa. For ease of purification and detection, a 23 amino acid His-tag is added to the N-terminus of the protein.
Shipped with Ice Packs
Cat. No.
BT11319
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

MDH2 Human

Malate Dehydrogenase 2 Human Recombinant

Recombinant human MDH2, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 335 amino acids (residues 25-338) with a molecular weight of 35.2 kDa. The MDH2 protein is fused to a 21 amino acid His tag at the N-terminus and purified using conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT11718
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

NQO1 Human

NAD(P)H Dehydrogenase Quinone 1 Human Recombinant

Recombinant human NQO1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain of 294 amino acids (residues 1-274), with a molecular weight of 33 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13805
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

NQO1 Human, Active

NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant

Recombinant human NQO1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 294 amino acids (residues 1-274) with a molecular weight of 33.0 kDa. It includes a 20 amino acid His tag at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT13873
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

GLDA E.coli

Glycerol dehydrogenase E.coli Recombinant

Recombinant GLDA from E.coli, expressed in E.Coli, is a single, non-glycosylated polypeptide chain containing 390 amino acids. A 23 amino acid His-tag is fused to the N-terminus of the 367 amino acid GLDA protein, resulting in a molecular mass of 41.1kDa. The protein has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8831
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GLDA E.coli, Active

Glycerol dehydrogenase E.coli Recombinant, Active

Recombinant GLDA from E. coli, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 390 amino acids (amino acids 1-367) and possessing a molecular weight of 41.1 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of GLDA, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT8916
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

IDH1

Isocitrate Dehydrogenase-1 Yeast Recombinant

This product consists of recombinant Saccharomyces Cerevisiae ICDH (NADP), a form of the enzyme derived from yeast cells specifically engineered for overexpression. This full-length protein is identical to the ICD1 enzyme found naturally in Saccharomyces Cerevisiae, with the exception of a single amino acid substitution (Phenylalanine to Alanine) near the N-terminal to enhance its production. The purification process involves advanced chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT10274
Source
Yeast cells.
Appearance
A clear solution that has been sterilized by filtration.

SORD Human

Sorbitol Dehydrogenase Human Recombinant

Recombinant human SORD, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 38.3 kDa. It consists of 357 amino acids (1-357) and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT14996
Source

Escherichia Coli.

Appearance
Clear, colorless solution, sterile-filtered.

SORD Human, His

Sorbitol Dehydrogenase Human Recombinant, His Tag

Recombinant human SORD, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 377 amino acids (specifically, amino acids 1 to 357). It possesses a molecular weight of 40.4 kDa. This protein is engineered with a 20 amino acid His tag at the N-terminus to facilitate purification via standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT15067
Source
Escherichia Coli.
Appearance
The product is a sterile-filtered solution that is colorless.

UGDH Human

UDP-Glucose Dehydrogenase Human Recombinant

Recombinant Human UGDH, expressed in E. coli, is available as a purified, non-glycosylated polypeptide chain. This protein consists of 533 amino acids, with a sequence encompassing residues 1-494, resulting in a molecular weight of 59.5 kDa. For purification and detection purposes, a 39 amino acid His-Tag is fused to the N-terminus. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT15148
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
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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