EPHX1 Human

Epoxide Hydrolase 1 Microsomal Human Recombinant

Recombinant human EPHX1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 451 amino acids (21-455a.a). With a molecular weight of 52.2kDa, it includes a 16 amino acid T7-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27425
Source
Escherichia Coli.
Appearance
A sterile, filtered solution that is colorless.

EPHX1 Human, Sf9

Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9

EPHX1, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 51.5 kDa. The recombinant protein consists of 442 amino acids, spanning residues 21 to 455, and includes a 6-amino acid His tag at the C-terminus to facilitate purification. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT27556
Source

Sf9, Insect cells.

Appearance
Clear, colorless solution, sterile-filtered.

FAAH2 Human

Fatty Acid Amide Hydrolase 2 Human Recombinant

Recombinant human FAAH2, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain. It consists of 524 amino acids (residues 32-532) and has a molecular weight of 57.4 kDa. The protein includes a 23 amino acid His-tag fused at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27632
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

FAHD1 Human

Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant

Recombinant human FAHD1, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a 20 amino acid His tag at the N-terminus. It consists of 244 amino acids (residues 1-224) and has a molecular weight of 27kDa. Purification of FAHD1 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27710
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PTRH2 Human

Peptidyl-tRNA Hydrolase 2 Human Recombinant

This product consists of the recombinant human PTRH2 protein, expressed in E. coli bacteria. A 21 amino acid His tag is fused to the N-terminus of the protein to facilitate purification. The resulting protein is a single, non-glycosylated polypeptide chain containing 137 amino acids (residues 64-179 of the full-length protein) with a molecular weight of 14.9 kDa. The PTRH2 protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28964
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PTRHD1 Human

Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant

Recombinant PTRHD1, of human origin, is produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 163 amino acids (1-140 a.a), with a molecular weight of 18.2 kDa. A 23 amino acid His-tag is fused to the N-terminus of PTRHD1. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29037
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered.

BPHL Human

Biphenyl Hydrolase-Like Human Recombinant

Produced in E. coli, our BPHL is a single, non-glycosylated polypeptide chain comprising 275 amino acids (residues 38-291). It has a molecular weight of 31.1 kDa. For purification, a 21 amino acid His-tag is fused to the N-terminus, and the protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27071
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

DDAH1 Human

Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant

Produced in E. coli, our recombinant DDAH1 protein is a non-glycosylated polypeptide chain consisting of 308 amino acids (residues 1-285) with a molecular weight of 33.5 kDa. It features a 23 amino acid His-tag fused to the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27156
Source
Escherichia Coli.
Appearance
Clear, sterile, and filtered solution.

ENTPD3 Human

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant

Recombinant human ENTPD3, expressed in E. coli, is a non-glycosylated polypeptide chain containing 465 amino acids (residues 44-485). It has a molecular weight of 52 kDa. A 23-amino acid His-tag is fused to the N-terminus, and the protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27238
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

ENTPD3 Human, sf9

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9

Recombinant human ENTPD3, expressed in Sf9 insect cells using a baculovirus system, is a single, non-glycosylated polypeptide chain. It comprises 451 amino acids (44-485a.a), resulting in a molecular weight of 50.7 kDa. On SDS-PAGE under reducing conditions, it migrates between 50-70 kDa. The protein is fused with a 6-amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27293
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.
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.

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