HADHB Human

2-Enoyl-Coenzyme A (CoA) Hydratase, Beta Human Recombinant

Recombinant HADHB protein, of human origin, is produced in E. coli. It is a single polypeptide chain that lacks glycosylation. This protein consists of 464 amino acids (with a sequence spanning from amino acid 34 to 474) and has a molecular weight of 49.9 kDa. For purification and enhanced solubility, a 23 amino acid His-tag is fused to the N-terminus of the HADHB protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT26214
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

PCBD1 Human

Pterin-4-Alpha-Carbinolamine Dehydratase Human Recombinant

Recombinant PCBD1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 124 amino acids (with amino acids 1-104 forming the PCBD1 sequence). It has a molecular weight of 14.1 kDa. The protein is purified using proprietary chromatographic techniques and is provided with an N-terminal 20 amino acid His-tag.
Shipped with Ice Packs
Cat. No.
BT26328
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GMDS Human

GDP-Mannose 4,6-Dehydratase Human Recombinant

Recombinant Human GMDS, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 44.1 kDa. It encompasses 392 amino acids, including a 20 amino acid His-tag at the N-terminus (amino acids 1-372). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26119
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ECHDC1 Human

Enoyl CoA Hydratase Domain Containing 1 Human Recombinant

Recombinant Human ECHDC1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 226 amino acids (specifically, amino acids 1 to 206), resulting in a molecular mass of 25.4 kDa. Notably, a 20 amino acid His Tag is fused to the N-terminus of ECHDC1. The purification process involves conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT25699
Source
E.coli.
Appearance
The product is a sterile, filtered solution that is colorless.

ECHS1 Human

Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant

Recombinant human ECHS1, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 284 amino acids (residues 28-290). With a molecular weight of 30.6 kDa, this protein is engineered with a 21 amino acid His-tag at the N-terminus to facilitate purification via proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25786
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

ECHS1 Human, Active

Enoyl CoA Hydratase, Short chain, 1, Mitochondrial, Human Recombinant, Active

Recombinant human ECHS1, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 284 amino acids (residues 28-290). With a molecular weight of 30.6 kDa, the protein includes a 21 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT25902
Source
Escherichia Coli.
Appearance
A clear solution, sterile-filtered.

ALAD Human

Aminolevulinate Dehydratase Human Recombinant

Recombinant human ALAD, produced in E. coli, is a single polypeptide chain with a molecular weight of 38.8kDa. It consists of 354 amino acids (1-330) and includes a 24 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25458
Source
E.coli.
Appearance
A sterile, colorless solution, free from particulate matter.

AUH Human

AU RNA Binding Protein/Enoyl-CoA Hydratase Human Recombinant

Recombinant AUH Human, fused with a 21 amino acid His tag at its N-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 293 amino acids (residues 68-339) and possesses a molecular weight of 31.4kDa. The purification of AUH is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25537
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ECH1 Human

Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant

Recombinant ECH1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 316 amino acids (residues 34-328) with a molecular weight of 34.4 kDa. It includes a 21 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25612
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

Fumarase Human

Fumarate Hydratase Human Recombinant

Recombinant Human Fumarase, expressed in E. coli, is a non-glycosylated polypeptide chain. This single-chain protein consists of 467 amino acids (residues 44-510) and has a molecular weight of 50.2 kDa. The purification process involves proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT26018
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
Definition and Classification

Hydratases are enzymes that catalyze the addition or removal of water molecules to or from substrates. They belong to the lyase family, specifically the hydro-lyases, which facilitate the cleavage of carbon-oxygen bonds by means other than hydrolysis or oxidation. Hydratases are classified based on their substrate specificity and the type of reaction they catalyze, such as fumarase, enoyl-CoA hydratase, and aconitase.

Biological Properties

Key Biological Properties: Hydratases are crucial for various metabolic pathways, including the citric acid cycle and fatty acid metabolism. They exhibit high substrate specificity and catalytic efficiency.

Expression Patterns: The expression of hydratases varies across different tissues and developmental stages. For instance, fumarase is highly expressed in the liver and kidneys, while enoyl-CoA hydratase is predominantly found in muscle tissues.

Tissue Distribution: Hydratases are ubiquitously distributed in both prokaryotic and eukaryotic organisms. They are present in various cellular compartments, including the cytoplasm, mitochondria, and peroxisomes.

Biological Functions

Primary Biological Functions: Hydratases play a pivotal role in metabolic processes. For example, fumarase catalyzes the reversible hydration of fumarate to malate in the citric acid cycle, while enoyl-CoA hydratase is involved in the β-oxidation of fatty acids.

Role in Immune Responses and Pathogen Recognition: Hydratases contribute to immune responses by modulating metabolic pathways that influence immune cell function. For instance, aconitase activity affects the production of reactive oxygen species, which are crucial for pathogen elimination.

Modes of Action

Mechanisms with Other Molecules and Cells: Hydratases interact with various substrates and cofactors to facilitate their catalytic activity. For example, aconitase requires an iron-sulfur cluster for its enzymatic function.

Binding Partners: Hydratases often form complexes with other enzymes or proteins to enhance their stability and activity. For instance, fumarase associates with other enzymes in the citric acid cycle to form a metabolon.

Downstream Signaling Cascades: The activity of hydratases can influence downstream signaling pathways. For example, the products of hydratase-catalyzed reactions can serve as signaling molecules that regulate cellular processes such as apoptosis and proliferation.

Regulatory Mechanisms

Transcriptional Regulation: The expression of hydratases is regulated at the transcriptional level by various transcription factors and signaling pathways. For instance, hypoxia-inducible factors can upregulate the expression of fumarase under low oxygen conditions.

Post-Translational Modifications: Hydratases undergo various post-translational modifications, such as phosphorylation and acetylation, which can modulate their activity, stability, and subcellular localization.

Applications

Biomedical Research: Hydratases are used as model enzymes to study metabolic pathways and enzyme kinetics. They also serve as targets for drug development in metabolic disorders and cancer.

Diagnostic Tools: The activity levels of certain hydratases can serve as biomarkers for diseases. For example, decreased fumarase activity is associated with fumarase deficiency, a rare metabolic disorder.

Therapeutic Strategies: Hydratases are potential therapeutic targets for various diseases. Inhibitors of enoyl-CoA hydratase are being explored as treatments for obesity and metabolic syndrome.

Role in the Life Cycle

Development: Hydratases are essential for embryonic development and cellular differentiation. For instance, aconitase activity is crucial for the proper development of the nervous system.

Aging: The activity of hydratases declines with age, contributing to metabolic dysregulation and age-related diseases. Enhancing hydratase activity is being explored as a strategy to promote healthy aging.

Disease: Dysregulation of hydratase activity is implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Understanding the role of hydratases in disease pathogenesis can inform the development of novel therapeutic approaches.

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