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 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10438
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

IMPDH2 Human

IMP Dehydrogenase 2 Human Recombinant

IMPDH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514) and having a molecular mass of 58kDa.
IMPDH2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10534
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

IVD Human

Isovaleryl Coenzyme A Dehydrogenase Human Recombinant

IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa.
The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Shipped with Ice Packs
Cat. No.
BT10629
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ldhA E. coli

Fermentative D-lactate Dehydrogenase, NAD-Dependent E.Coli Recombinant

ldhA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1kDa.
ldhA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10721
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LDHA Human

Lactate Dehydrogenase A Human Recombinant

LDHA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-332 a.a.) and having a molecular mass of 38.8 kDa. The LDHA is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Shipped with Ice Packs
Cat. No.
BT10801
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LDHA Mouse

Lactate Dehydrogenase A Mouse Recombinant

LDHA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332a.a.) and having a molecular mass of 37.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
LDHA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10857
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

LDHA Rat

Lactate Dehydrogenase A, Rat Recombinant

LDHA Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332 a.a) and having a molecular mass of 37.5kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). 
LDHA is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10929
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

LDHA, E.Coli Active

Lactate Dehydrogenase A, BioActive E.Coli Recombinant

LDHA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1 kDa.
LDHA E.Coli is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11019
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless solution.

LDHB

Lactate Dehydrogenase B Recombinant

The DNA encoding chicken LDH-B is cloned from cDNA library of chicken heart.
Shipped with Ice Packs
Cat. No.
BT11071
Source
Escherichia Coli.
Appearance
Sterile lyophilized powder.

LDHB Human

Lactate Dehydrogenase B Human Recombinant

LDHB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-334) and having a molecular mass of 36.6kDa.
Shipped with Ice Packs
Cat. No.
BT11181
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless 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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