CES1 Human

Carboxylesterase 1 Human Recombinant

CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17700
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

ACHE Human

Acetylcholinesterase Human Recombinant

ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa.
ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17752
Source

HEK293 Cells.

Appearance

Sterile Filtered colorless solution.

ACOT11 Human

Acyl-CoA Thioesterase 11 Human Recombinant

ACOT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 268 amino acids (19-250 a.a) and having a molecular mass of 29.9kDa. ACOT11 is fused to a 36 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT17913
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ACOT13 Human

Acyl-CoA Thioesterase 13 Human Recombinant

ACOT13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.1kDa. The ACOT13 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17994
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ACOT7 Human

Acyl-CoA Thioesterase 7 Human Recombinant

ACOT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-370) and having a molecular mass of 42.6kDa.
ACOT7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18089
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ACOT8 Human

Acyl-CoA Thioesterase 8 Human Recombinant

ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18184
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CES1D Mouse

Carboxylesterase 1D Mouse Recombinant

CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18268
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

CES1G Mouse

Carboxylesterase 1G Mouse Recombinant

CES1G produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 556 amino acids (19-565 a.a.) and having a molecular mass of 61.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).
CES1G is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18340
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

Esterase D Human

Esterase D,S-Formylglutathione Hydrolase Human Recombinant

Esterase-D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 302 amino acids (1-282 a.a.) and having a molecular mass of 33.6kDa.
The Esterase-D is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18428
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PDE6D Human

Phosphodiesterase 6D cGMP-Specific Rod Delta Human Recombinant

PDE6D produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-150 a.a.) and having a molecular mass of 18.4kDa. PDE6D is fused to an 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18486
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
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 .
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