Enzymes
Product List
BLMH Mouse
Bleomycin Hydrolase Mouse Recombinant
BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.
BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Escherichia Coli.
BPHL Human
Biphenyl Hydrolase-Like Human Recombinant
BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
DDAH1 Human
Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant
DDAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ENTPD3 Human
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant
ENTPD3 Human, sf9
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9
ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.
ENTPD3 Human, sf9 Bioactive
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
EPHX1 Human
Epoxide Hydrolase 1 Microsomal Human Recombinant
EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa.
EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.
EPHX1 Human, Sf9
Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9
EPHX1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 442 amino acids (21-455 a.a.) and having a molecular mass of 51.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
EPHX1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Insect cells.
FAAH2 Human
Fatty Acid Amide Hydrolase 2 Human Recombinant
FAHD1 Human
Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant
Introduction
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.
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.
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.
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: 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.
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 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.
