GAPDH Mouse

GAPDH Mouse Recombinant

GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.
GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8595
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

GAPDH Mouse, Active

GAPDH Mouse Recombinant, Active

GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.
GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8654
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

GCDH Human

Glutaryl-Coenzyme A Dehydrogenase Human Recombinant

GCDH Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (45-438 a.a.) and having a molecular mass of 45.8 kDa. The GCDH is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8747
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GLDA E.coli

Glycerol dehydrogenase E.coli Recombinant

GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8831
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GLDA E.coli, Active

Glycerol dehydrogenase E.coli Recombinant, Active

GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8916
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GLUD1 Human

Glutamate Dehydrogenase 1 Human Recombinant

GLUD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (54-558) and having a molecular mass of 58.4kDa.
GLUD1 is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT9155
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GPD1 Human

Glycerol-3-Phosphate Dehydrogenase 1 Human Recombinant

GPD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349 a.a.) and having a molecular mass of 37.5 kDa. The GPD1 is purified by conventional chromatography.
Shipped with Ice Packs
Cat. No.
BT9229
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GPD1L Human

Glycerol-3-Phosphate Dehydrogenase 1 Like Human Recombinant

GPD1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-351 a.a.) and having a molecular mass of 40.6kDa.
GPD1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9330
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GPD2 Human

Glycerol-3-Phosphate Dehydrogenase 2 Human Recombinant

GPD2 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 558 amino acids fragment (43-600) corresponding to the GlpA domain fragment of the mature protein, having a total molecular mass of 66.26kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The GPD2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9423
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

HADH Human

Hydroxyacyl-Coenzyme A Dehydrogenase Human Recombinant

HADH Human Recombinant fused to a 21 amino acids His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (13-314 a.a.) and having a molecular mass of 35.1 kDa. The HADH is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9489
Source
Escherichia Coli.
Appearance
Sterile Filtered clear 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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