Product List

ALAD Human

Aminolevulinate Dehydratase Human Recombinant

ALAD Human Recombinant produced in E. coli is a single polypeptide chain containing 354 amino acids (1-330) and having a molecular mass of 38.8kDa.
ALAD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25458
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

AUH Human

AU RNA Binding Protein/Enoyl-CoA Hydratase Human Recombinant

AUH Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (68-339 a.a.) and having a molecular mass of 31.4kDa. The AUH is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25537
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ECH1 Human

Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant

ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.
ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25612
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ECHDC1 Human

Enoyl CoA Hydratase Domain Containing 1 Human Recombinant

SNAP25 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-206 a.a.) and having a molecular mass of 25.4 kDa.
SNAP25 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT25699
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

ECHS1 Human

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

ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.
ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25786
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

ECHS1 Human, Active

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

ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a) and having a molecular mass of 30.6kDa. ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT25902
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Fumarase Human

Fumarate Hydratase Human Recombinant

Fumarase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 467 amino acids (44-510) and having a molecular mass of 50.2 kDa.
Fumarate Hydratase is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26018
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GMDS Human

GDP-Mannose 4,6-Dehydratase Human Recombinant

GMDS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-372) and having a molecular mass of 44.1 kDa.
GMDS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26119
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

HADHB Human

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

HADHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (34-474 a.a) and having a molecular mass of 49.9kDa. HADHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26214
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PCBD1 Human

Pterin-4-Alpha-Carbinolamine Dehydratase Human Recombinant

PCBD1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 124 amino acids (1-104 a.a.) and having a molecular mass of 14.1kDa.
PCBD1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26328
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Introduction

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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