Enzymes
Product List
ENPP1 Mouse
Ectonucleotide Pyrophosphatase Mouse Recombinant
ENPP1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 828 amino acids (Lys85-Glu906) and having a molecular mass of 95.2kDa.
ENPP1 Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Filtered White lyophilized (freeze-dried) powder.
ENPP2 Human
Ectonucleotide Pyrophosphatase-2 Human Recombinant
ENPP2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 825 amino acids (49-863a.a) and having a molecular mass of 94.9kDa.
ENPP2 is fused to a 6 amino acid His-tag at C-terminus, and is purified by proprietary chromatographic techniques.
FBP1 Human
Fructose-1,6-Bisphosphatase 1 Human Recombinant
The FBP1 enzyme is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.
FBP1 Human, Active
Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant
FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.
FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Escherichia Coli.
FBP2 Human
Fructose-1,6-Bisphosphatase 2 Human Recombinant
IMPA1 Human
Inositol Monophosphatase 1 Human Recombinant
IMPA2 Human
Inositol Monophosphatase 2 Human Recombinant
ITPA Human
Inosine Triphosphatase Human Recombinant
The ITPA is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
LHPP Human
Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant
LHPP is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MDP1 Human
Magnesium-Dependent Phosphatase 1 Human Recombinant
MDP1 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 200 amino acids (1-176 a.a.) and having a molecular mass of 22.6kDa. The MDP1 is purified by proprietary chromatographic techniques.
Introduction
Phosphatases are a group of enzymes that catalyze the removal of phosphate groups from molecules, a process known as dephosphorylation. They play a crucial role in various cellular processes by regulating the phosphorylation state of proteins and other molecules. Phosphatases are broadly classified into two main categories:
- Protein Phosphatases: These enzymes specifically target phosphorylated amino acid residues in proteins. They are further divided into:
- Serine/Threonine Phosphatases: Target serine or threonine residues.
- Tyrosine Phosphatases: Target tyrosine residues.
- Dual-Specificity Phosphatases: Can target both serine/threonine and tyrosine residues.
- Non-Protein Phosphatases: These enzymes act on non-protein substrates, such as nucleotides, sugars, and lipids.
Key Biological Properties:
- Catalytic Activity: Phosphatases hydrolyze phosphate esters, releasing inorganic phosphate.
- Substrate Specificity: They exhibit specificity for their substrates, which can be proteins, nucleotides, or other molecules.
Expression Patterns:
- Phosphatases are ubiquitously expressed in various tissues and cell types, with specific isoforms showing distinct expression patterns.
Tissue Distribution:
- Protein Phosphatases: Widely distributed across tissues, with high expression in the brain, liver, and muscles.
- Non-Protein Phosphatases: Found in various tissues, depending on their specific substrates.
Primary Biological Functions:
- Regulation of Signal Transduction: Phosphatases modulate signaling pathways by dephosphorylating key signaling molecules.
- Cell Cycle Control: They play a role in cell cycle progression by regulating the phosphorylation state of cell cycle proteins.
- Metabolic Regulation: Phosphatases are involved in metabolic pathways by dephosphorylating metabolic enzymes.
Role in Immune Responses:
- Phosphatases regulate immune cell activation and function by modulating signaling pathways involved in immune responses.
Pathogen Recognition:
- Some phosphatases are involved in recognizing and responding to pathogen-associated molecular patterns (PAMPs), contributing to the immune defense.
Mechanisms with Other Molecules and Cells:
- Phosphatases interact with various molecules, including proteins, lipids, and nucleotides, to exert their dephosphorylation activity.
Binding Partners:
- They often form complexes with other proteins, which can regulate their activity and substrate specificity.
Downstream Signaling Cascades:
- By dephosphorylating key signaling molecules, phosphatases influence downstream signaling pathways, affecting cellular responses such as proliferation, differentiation, and apoptosis.
Regulatory Mechanisms:
- Transcriptional Regulation: The expression of phosphatases is regulated at the transcriptional level by various transcription factors and signaling pathways.
- Post-Translational Modifications: Phosphatases themselves can be regulated by post-translational modifications, such as phosphorylation, ubiquitination, and methylation, which can alter their activity, stability, and localization.
Biomedical Research:
- Phosphatases are studied to understand their role in various diseases, including cancer, diabetes, and neurodegenerative disorders.
Diagnostic Tools:
- Phosphatase activity assays are used in diagnostic tests to measure enzyme activity in biological samples, aiding in the diagnosis of certain diseases.
Therapeutic Strategies:
- Inhibitors of specific phosphatases are being developed as potential therapeutic agents for diseases where phosphatase activity is dysregulated.
Role Throughout the Life Cycle:
- Development: Phosphatases are involved in embryonic development by regulating signaling pathways that control cell differentiation and tissue formation.
- Aging: Changes in phosphatase activity have been associated with aging and age-related diseases, such as Alzheimer’s disease.
- Disease: Dysregulation of phosphatase activity is implicated in various diseases, including cancer, where altered phosphorylation states can lead to uncontrolled cell growth and proliferation.
