ENTPD3 Human, sf9 Bioactive

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive

Recombinant human ENTPD3, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It comprises 451 amino acids (44-485a.a.) with a molecular mass of 50.7 kDa. On SDS-PAGE, the apparent molecular size will be approximately 50-70 kDa due to glycosylation. The protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27371
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.

HIBCH Human

3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant

Recombinant HIBCH, produced in E. coli, is a single polypeptide chain consisting of 379 amino acids (residues 33-386) with a molecular weight of 42.1 kDa. This protein is fused to a 25 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28632
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LTA4H Human

Leukotriene A4 Hydrolase Human Recombinant

Recombinant human LTA4H, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 634 amino acids (1-611 a.a). It has a molecular mass of 71.7kDa. A 23 amino acid His-tag is fused to the N-terminus of LTA4H, and it is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28713
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.

PAFAH1B3 Human

Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant

Recombinant human PAFAH1B3, expressed in E. coli, is a single polypeptide chain comprising 254 amino acids (1-231) with a molecular weight of 28.2 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28785
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ADPRH Human

ADP-Ribosylarginine Hydrolase Human Recombinant

This product consists of the recombinant human ADPRH enzyme, produced in E.coli. It is a single, non-glycosylated polypeptide chain with 381 amino acids (residues 1-357) and a molecular weight of 42.1 kDa. The enzyme has a His-tag fused to its N-terminus for purification purposes. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26700
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ADPRHL2 Human

ADP-Ribosylhydrolase Like 2 Human Recombinant

Recombinant human ADPRHL2, expressed in E. coli, is a single polypeptide chain with a molecular weight of 41.5 kDa. The protein consists of 387 amino acids, with a truncated sequence spanning residues 1 to 363. A 24 amino acid His-tag is fused to the N-terminus to facilitate purification, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26803
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

BLMH Human

BLM Hydrolase Human Recombinant

Recombinant BLMH, expressed in E. coli, is produced as a single, non-glycosylated polypeptide chain comprising 475 amino acids (residues 1-455). With a molecular weight of 54.7 kDa, the protein features a 20 amino acid His-tag fused at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26895
Source
Escherichia Coli.
Appearance
Sterile, clear solution.

BLMH Mouse

Bleomycin Hydrolase Mouse Recombinant

Recombinant BLMH Mouse, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain. It consists of 478 amino acids, encompassing residues 1-455, and has a molecular weight of 54.9 kDa. The N-terminus of BLMH is fused to a 23 amino acid His-tag. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26988
Source

Escherichia Coli.

Appearance
Clear, colorless solution, sterile-filtered.

HAGH Human

Hydroxyacylglutathione Hydrolase Human Recombinant

Recombinant human HAGH protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing 284 amino acids (residues 1-260). The protein has a molecular weight of 31.4 kDa and includes an N-terminal 24 amino acid His-tag to facilitate purification. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28211
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

HDDC3 Human

HD domain containing 3 Human Recombinant

Recombinant human HDDC3, expressed in E. coli, is a purified protein with a molecular weight of 17.9 kDa. It consists of a single polypeptide chain of 160 amino acids, with the first 140 amino acids representing the HDDC3 protein and a 20 amino acid His-tag fused at the N-terminus to facilitate purification. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT28273
Source
Escherichia Coli.
Appearance
Clear, colorless solution without any visible particles.
Definition and Classification

Hydrolases are a class of enzymes that catalyze the hydrolysis of chemical bonds. These enzymes are essential for various biological processes, as they facilitate the breakdown of complex molecules into simpler ones by adding water. Hydrolases are classified based on the type of bond they act upon:

  • Esterases: Hydrolyze ester bonds.
  • Glycosidases: Hydrolyze glycosidic bonds in carbohydrates.
  • Peptidases: Hydrolyze peptide bonds in proteins.
  • Lipases: Hydrolyze lipid molecules.
  • Phosphatases: Hydrolyze phosphate esters.
Biological Properties

Key Biological Properties: Hydrolases exhibit high specificity for their substrates and operate under mild physiological conditions. They are often regulated by factors such as pH, temperature, and the presence of cofactors or inhibitors.

Expression Patterns: The expression of hydrolases varies widely among different organisms and tissues. Some hydrolases are constitutively expressed, while others are inducible in response to specific stimuli.

Tissue Distribution: Hydrolases are distributed throughout various tissues in the body. For example, digestive hydrolases like amylase and lipase are predominantly found in the pancreas and salivary glands, while lysosomal hydrolases are present in almost all cell types.

Biological Functions

Primary Biological Functions: Hydrolases play crucial roles in metabolism, digestion, and cellular maintenance. They are involved in the degradation of macromolecules, recycling of cellular components, and energy production.

Role in Immune Responses: Certain hydrolases, such as lysozyme, are involved in the immune response by breaking down the cell walls of pathogens, thereby aiding in pathogen recognition and destruction.

Pathogen Recognition: Hydrolases can recognize and degrade pathogen-associated molecular patterns (PAMPs), which are essential for the innate immune response.

Modes of Action

Mechanisms with Other Molecules and Cells: Hydrolases interact with various molecules and cells to exert their effects. For instance, digestive hydrolases break down dietary macromolecules into absorbable units.

Binding Partners: Hydrolases often require specific binding partners or cofactors to function effectively. For example, many hydrolases require metal ions like zinc or magnesium for catalytic activity.

Downstream Signaling Cascades: The activity of hydrolases can trigger downstream signaling cascades that regulate various cellular processes. For example, the hydrolysis of phosphoinositides by phospholipase C generates second messengers that modulate cellular signaling pathways.

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of hydrolases are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.

Transcriptional Regulation: The transcription of hydrolase genes can be regulated by various transcription factors in response to environmental cues or cellular signals.

Post-Translational Modifications: Hydrolases can undergo post-translational modifications such as phosphorylation, glycosylation, and ubiquitination, which can alter their activity, stability, and localization.

Applications

Biomedical Research: Hydrolases are widely used in biomedical research to study metabolic pathways, disease mechanisms, and cellular processes.

Diagnostic Tools: Hydrolases serve as biomarkers for various diseases. For example, elevated levels of certain hydrolases in the blood can indicate liver or pancreatic disorders.

Therapeutic Strategies: Hydrolases are employed in therapeutic strategies, such as enzyme replacement therapy for lysosomal storage diseases and the use of proteases in wound debridement.

Role in the Life Cycle

Role Throughout the Life Cycle: Hydrolases play vital roles throughout the life cycle, from development to aging and disease. During development, hydrolases are involved in tissue remodeling and differentiation. In adulthood, they maintain cellular homeostasis and metabolic balance. In aging and disease, dysregulation of hydrolase activity can contribute to pathological conditions such as neurodegeneration and cancer.

© Copyright 2025 TheBiotek. All Rights Reserved.