LDHA, E.Coli Active

Lactate Dehydrogenase A, BioActive E.Coli Recombinant

Recombinant LDHA from E.Coli is a single, non-glycosylated polypeptide chain. It consists of 353 amino acids (amino acids 1-329) and has a molecular weight of 39.1 kDa.
This LDHA protein is fused to a 24 amino acid His-Tag at its N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11019
Source

Escherichia Coli.

Appearance
A sterile, filtered solution without any color.

LDHB

Lactate Dehydrogenase B Recombinant

This product contains the LDH-B gene from chicken heart. The gene was obtained from a cDNA library.
Shipped with Ice Packs
Cat. No.
BT11071
Source
Escherichia Coli.
Appearance
Dry powder, free from bacteria.

LDHB Human

Lactate Dehydrogenase B Human Recombinant

Recombinant human LDHB, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 334 amino acids (1-334). It has a molecular weight of 36.6 kDa.
Shipped with Ice Packs
Cat. No.
BT11181
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for purity.

ACAD8 Human

Acyl-Coenzyme A Dehydrogenase 8 Human Recombinant

Recombinant human ACAD8, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 416 amino acids (23-415) and possessing a molecular mass of 45.1 kDa. It includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6222
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

ACADL Human

Acyl-CoA Dehydrogenase, Long Chain, Human Recombinant

Recombinantly produced in E.coli, ACADL Human Recombinant is a single, non-glycosylated polypeptide chain. It consists of 421 amino acids (31-430) and has a molecular weight of 46.7 kDa. The protein features a 21 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6296
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

ALDH2 Mouse

Aldehyde Dehydrogenase 2 Mouse Recombinant

This product consists of the recombinant mouse ALDH2 protein. It is a single, non-glycosylated polypeptide chain containing 523 amino acids (amino acids 20-519) with a molecular weight of 56.8 kDa. The protein is produced in E. coli and purified using proprietary chromatographic techniques. For ease of purification and detection, a 23 amino acid His-tag is fused to the N-terminus of the protein.
Shipped with Ice Packs
Cat. No.
BT7339
Source
Escherichia Coli.
Appearance
A clear solution free from particulate matter after sterilization by filtration.

IVD Human

Isovaleryl Coenzyme A Dehydrogenase Human Recombinant

This product consists of the human IVD enzyme, produced recombinantly in E. coli bacteria. It is engineered without any glycosylation (addition of sugar molecules) and exists as a single polypeptide chain of 415 amino acids. This includes amino acids 33 to 426 of the native human IVD protein, along with an additional 20 amino acid histidine tag at the N-terminus to facilitate purification. The purified protein has a molecular weight of approximately 45.3 kDa.
Shipped with Ice Packs
Cat. No.
BT10629
Source
Escherichia Coli.
Appearance
Clear and colorless liquid, sterilized by filtration.

ldhA E. coli

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

Recombinant ldhA from E. coli is a single, non-glycosylated polypeptide chain consisting of 353 amino acids (residues 1-329). It has a molecular weight of 39.1 kDa. This ldhA protein is expressed with a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10721
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

LDHA Human

Lactate Dehydrogenase A Human Recombinant

Recombinant human LDHA is a 38.8 kDa protein containing 352 amino acids (1-332 a.a.), including a 20 amino acid histidine tag at the N-terminus. It is produced in E. coli and purified to a high degree using conventional chromatography techniques. The recombinant LDHA is a single, non-glycosylated polypeptide chain, ensuring homogeneity and consistency for research applications.
Shipped with Ice Packs
Cat. No.
BT10801
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

LDHA Mouse

Lactate Dehydrogenase A Mouse Recombinant

Recombinant LDHA Mouse protein, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 37.5kDa (as determined by mass spectrometry). It encompasses 340 amino acids, including an 8 amino acid His tag at the C-terminus (1-332a.a.). Purification is achieved using proprietary chromatographic techniques. Due to glycosylation, the protein may appear between 28-40kDa on SDS-PAGE.
Shipped with Ice Packs
Cat. No.
BT10857
Source
Sf9, Baculovirus cells.
Appearance
A 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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