HSD17B1 Human

Hydroxysteroid (17-beta) Dehydrogenase 1 Human Recombinant

Recombinant human HSD17B1, expressed in E. coli, is a non-glycosylated polypeptide chain. This single-chain protein consists of 352 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-328), resulting in a molecular weight of 37.5 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9904
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

HSD17B10 Human

Hydroxysteroid (17-beta) Dehydrogenase 10 Human Recombinant

Recombinant HSD17B10, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 271 amino acids (residues 12-261). With a molecular weight of 28.1 kDa, this protein is produced with a 21-amino acid His-Tag fused at the N-terminus to facilitate purification via standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT9996
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for purity.

HSD17B11 Human

Hydroxysteroid (17-beta) Dehydrogenase 11 Human Recombinant

Recombinant human HSD17B11, expressed in E. coli with an N-terminal 21 amino acid His tag, is a single, non-glycosylated polypeptide chain. It consists of 287 amino acids (20-285 a.a.), resulting in a molecular weight of 31.4 kDa. Purification of HSD17B11 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10098
Source
Escherichia Coli.
Appearance
Sterile filtered, colorless solution.

HSD17B14 Human

Hydroxysteroid (17-beta) Dehydrogenase 14 Human Recombinant

This product is a recombinant human HSD17B14 protein. It is produced in E. coli and includes a 36 amino acid His tag fused at the N-terminus. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 32.4 kDa. It consists of 306 amino acids, with residues 1-270 representing the HSD17B14 sequence. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10148
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

HSD17B8 Human

Hydroxysteroid (17-beta) Dehydrogenase 8 Human Recombinant

Recombinant human HSD17B8, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 281 amino acids (amino acids 1-261), with a molecular weight of 29.1 kDa. The protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10210
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

lldD E. coli

L-Lactate Dehydrogenase E.Coli Recombinant

Recombinant lldD from E. coli is produced as a single, non-glycosylated polypeptide chain. It consists of 420 amino acids (residues 1-396), resulting in a molecular weight of 45.3 kDa. The protein includes an N-terminal 24 amino acid His-tag and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11429
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

MDH E. coli

Malate Dehydrogenase Recombinant

This recombinant MDH, produced in E. coli, is a single polypeptide chain consisting of 336 amino acids (with the first 312 amino acids forming the MDH sequence). It has a molecular weight of 34.9 kDa. For purification purposes, a 24 amino acid His-tag is attached to the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11520
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

MDH1 Chicken

Malate Dehydrogenase Chicken Recombinant

This product consists of Malate Dehydrogenase (MDH1) derived from chicken heart. The encoding gene for MDH1 was cloned from a chicken heart cDNA library. After expression, the enzyme is purified using advanced chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT11590
Source
Escherichia Coli.
Appearance
Provided as a sterile powder that has been freeze-dried.

MDH1 Human

Malate Dehydrogenase 1 Human Recombinant

Recombinant human MDH1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 342 amino acids, with amino acids 1-334 representing the MDH1 sequence. The protein has a molecular weight of 37.4 kDa and includes an 8 amino acid His tag fused to the C-terminus. Purification is achieved using conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT11643
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

NDUFAF4 Human

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 4 Human Recombinant

Recombinant human NDUFAF4, expressed in E. coli, is a non-glycosylated polypeptide chain containing 198 amino acids (1-175) with a molecular weight of 22.7 kDa. It 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.
BT12937
Source
Escherichia Coli.
Appearance
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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