LDHA Rat

Lactate Dehydrogenase A, Rat Recombinant

Recombinant LDHA from Rat, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 340 amino acids (1-332 a.a). It has a molecular mass of 37.5kDa and migrates at 28-40kDa on SDS-PAGE under reducing conditions. This protein is fused to an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10929
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NDUFAF1 Human

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant

Recombinant human NDUFAF1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 326 amino acids (residues 25-327) and has a molecular weight of 37 kDa. The protein includes a 23 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12151
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

NDUFAF2 Human

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant

Recombinant NDUFAF2 protein, expressed in E. Coli, is a single polypeptide chain devoid of glycosylation. It comprises 189 amino acids, with a sequence spanning from position 1 to 169, and possesses a molecular weight of 22kDa. For purification purposes, a 20 amino acid His-tag is fused to the N-terminus, and the protein is subsequently purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12268
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that appears colorless.

NDUFV2 Human

NADH Dehydrogenase Flavoprotein 2 Human Recombinant

This product consists of the recombinant human NDUFV2 protein. It is produced in E. coli and is engineered for clarity and ease of use in research. The protein is not glycosylated, meaning it lacks sugar modifications, and comprises a single polypeptide chain of 240 amino acids. This specific sequence spans from amino acid positions 33 to 249. With a molecular weight of 26.1 kDa, the NDUFV2 protein is further modified for experimental utility. It features a 23 amino acid His-tag attached to its N-terminus, facilitating purification through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13596
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized through filtration.

NDUFV3 Human

NADH Dehydrogenase Flavoprotein 3 Human Recombinant

Recombinant Human NDUFV3, expressed in E. coli, is a non-glycosylated polypeptide chain with a single chain. It consists of 97 amino acids (residues 35-108) and has a molecular weight of 10.8 kDa. The N-terminus of NDUFV3 is fused to a 23 amino acid His-tag. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13696
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized through filtration.

ALDH2 Mouse, Active

Aldehyde Dehydrogenase 2 Mouse Recombinant, Active

This recombinant ALDH2 protein was expressed in E. coli and purified. It is a single, non-glycosylated polypeptide chain with a molecular weight of 56.8 kDa. The protein sequence includes amino acids 20-519 of the mouse ALDH2 protein, along with a 23 amino acid His-tag at the N-terminus.

Purification was achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7401
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

ALDH3A1 Human

Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant

Recombinantly produced in E. coli, ALDH3A1 Human Recombinant is a single, non-glycosylated polypeptide chain comprising 473 amino acids (specifically, amino acids 1 to 453). With a molecular weight of 52.5 kDa, this protein features a 20 amino acid His Tag fused at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7475
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ALDH5A1 Human

Aldehyde Dehydrogenase 5 A1 Human Recombinant

This product consists of the human ALDH5A1 protein, recombinantly produced in E. coli. It is a single, non-glycosylated polypeptide chain, with a His tag attached to its N-terminus. The protein encompasses amino acids 48 to 535, resulting in a molecular weight of 54.6 kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7538
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ALDH6A1 Human

Aldehyde Dehydrogenase 6 A1 Human Recombinant

This product consists of ALDH6A1, a human recombinant protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain with 525 amino acids (specifically, amino acids 34 to 535) and a molecular weight of 56.8 kDa. The protein includes a 23 amino acid His-tag at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7631
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

LDHB Human, His

Lactate Dehydrogenase B Human Recombinant, His Tag

Recombinant Human LDHB, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 354 amino acids, including a 20 amino acid His-Tag fused at the N-terminus (1-334 a.a.), and has a molecular weight of 38.8 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11251
Source
Escherichia Coli.
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.