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Enzymes

Esterase

Creatine Kinases

Isomerase

Phosphatase

TPA

TGFBR

Transaminase

Cyclin-Dependent Kinase

PPARG

PI3-kinase

Transferase

Cyclin

Phosphorylase

Cyclophilin

Jun N-terminal Kinase

Jun Proto-Oncogene

Polymerase

Kallikrein

Protease

Deaminase

Ligase

Proteasome

Lipase

Decarboxylase

Lipocalin

Dehydrogenase

Lyase

LYVE1

MMP

Protein Kinase-A

Protein Kinase-C

Protein Kinase Akt1/PKB alpha

Protein Kinases

TIMP

Mitogen-Activated Protein Kinase

Mutase

Natural Enzymes

Nuclease

Discoidin Domain Receptor Tyrosine Kinase

DNA Polymerase

TGM2

Reductase

EGF Receptor

Nucleotidase

Tyrosine Kinase

Endonuclease

Nudix Type Motif

Enolase

Ubiquitin Conjugating Enzyme

Enterokinase

Epimerase

Oxidase

FGF Receptors

Oxygenase

FK506 Binding Protein

Uromodulin

VEGF Receptors

Fructosamine 3 Kinase

Paraoxonase

Galactosidase

Peptidase

Secreted Phospholipase A2

Glucosidase

Gluteradoxin

Other Enzymes

Serine Threonine Kinase

Glycogen synthase kinase

Sulfatase

Glycosylase

Synthase

Glyoxalase

Granzyme

ACE2

Guanylate Kinase

Hexokinase

Peroxiredoxin

Activating Transcription Factor

Histone Deacetylase

Adenylate Kinase

Heparanase

Protein Tyrosine Phosphatase

Hydratase

Synthetase

AHCY

Aldolase

Hydrolase

Alkaline Phosphatase

Asparaginase

Aurora Kinase

Beta Lactamase

Calcium/Calmodulin-Dependent Protein Kinase

TIE1,TIE2

Calcium and Integrin Binding

Carbonic Anhydrase

Hydroxylase

Casein Kinase

Cathepsin

Chitinase

Product List

TDP1 Human

Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant

Recombinant human TDP1, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 318 amino acids (residues 1-298) with a molecular weight of 35.8 kDa. It includes an N-terminal 20 amino acid His-tag and is purified using proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT18652

Source

Escherichia Coli.

Appearance

A clear, sterile solution without any color.

View Details

CES1 Human

Carboxylesterase 1 Human Recombinant

Recombinant CES1, human, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 61.7 kDa. The protein encompasses amino acids 19-568, incorporating a 9-amino acid His tag at the C-terminus. Purification is achieved using proprietary chromatographic techniques. On SDS-PAGE, the apparent molecular size may appear between 50-70 kDa due to glycosylation.

Shipped with Ice Packs

Cat. No.

BT17700

Source

Sf9, Baculovirus cells.

Appearance

Sterile, colorless solution.

View Details

ACHE Human

Acetylcholinesterase Human Recombinant

Recombinant human ACHE, produced in HEK cells, is a single, glycosylated polypeptide chain with a molecular weight of 65.6 kDa. The chain consists of 592 amino acids (32-614 a.a). The ACHE protein has a 6 amino acid His-tag fused at its C-terminus and undergoes purification using proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT17752

Source

HEK293 Cells.

Appearance

The product is a colorless solution that has been sterilized by filtration.

View Details

TDP2 Human

Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant

Recombinant human TDP2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 385 amino acids (residues 1-362) with a molecular weight of 43.3 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.

Shipped with Ice Packs

Cat. No.

BT18818

Source

Escherichia Coli.

Appearance

A clear, sterile solution without any color.

View Details

YOD1 Human

YOD1 Human Recombinant

Recombinant human YOD1, expressed in E.coli, is a non-glycosylated polypeptide chain with a molecular weight of 40.7kDa. This single chain protein comprises 371 amino acids, including a 23 amino acid His-tag fused at the N-terminus (amino acids 1-348). Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT18917

Source

Escherichia Coli.

Appearance

Clear, colorless, and sterile-filtered solution.

View Details

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Introduction

Definition and Classification

Esterases are a class of hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into an acid and an alcohol through a reaction with water. They are classified based on their substrate specificity and protein structure. The main types include:

Carboxylic ester hydrolases: e.g., acetylesterase, cholinesterase, pectinesterase.
Thiolester hydrolases: e.g., thioesterase.
Phosphoric monoester hydrolases: e.g., phosphatase.
Phosphoric diester hydrolases.
Sulfuric ester hydrolases: e.g., sulfatases.

Biological Properties

Esterases exhibit diverse biological properties, including broad substrate specificity and stability under various conditions. They are expressed in multiple tissues, including the liver, blood plasma, and various microbial environments. Their tissue distribution is extensive, with significant roles in lipid metabolism and detoxification processes.

Biological Functions

Esterases play crucial roles in various biological functions:

Lipid Metabolism: They hydrolyze lipid esters, aiding in lipid absorption and metabolism.
Detoxification: Esterases help in the breakdown of xenobiotic compounds, contributing to detoxification.
Immune Responses: Certain esterases are involved in pathogen recognition and immune responses.

Modes of Action

Esterases interact with other molecules and cells through specific binding partners and downstream signaling cascades. The catalytic mechanism typically involves a serine residue in the active site, which attacks the carbonyl carbon of the ester bond, facilitated by histidine and aspartic/glutamic acid residues. This leads to the formation of an acyl-enzyme intermediate, which is subsequently hydrolyzed to release the products.

Regulatory Mechanisms

The expression and activity of esterases are regulated through various mechanisms:

Transcriptional Regulation: Gene expression is controlled by transcription factors and regulatory elements in the promoter regions.
Post-Translational Modifications: Esterase activity can be modulated by phosphorylation, glycosylation, and other modifications.
Environmental Factors: pH, temperature, and the presence of inhibitors or activators can influence esterase activity.

Applications

Esterases have numerous applications in biomedical research, diagnostics, and therapeutics:

Biomedical Research: Used as tools to study lipid metabolism and enzyme kinetics.
Diagnostic Tools: Employed in assays to detect specific ester substrates or products.
Therapeutic Strategies: Targeted for drug development, particularly in the treatment of metabolic disorders and detoxification therapies.

Role in the Life Cycle

Throughout the life cycle, esterases play vital roles from development to aging and disease:

Development: Involved in the regulation of lipid metabolism during growth and development.
Aging: Changes in esterase activity are associated with aging processes and age-related diseases.
Disease: Altered esterase activity is linked to various diseases, including metabolic disorders, neurodegenerative diseases, and cancer.