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Product List
ACP2 Human
Acid Phosphatase-2 Human Recombinant
ACP2 Human Recombinant protein is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 373 amino acids (residues 31-380) with a molecular mass of 42.9 kDa. The protein is fused to a 23 amino acid His-Tag at the N-terminus and purified using conventional chromatography techniques.
Shipped with Ice Packs 
DUSP13 Human
Dual Specificity Phosphatase 13 Human Recombinant
Recombinantly produced in E. coli, DUSP13 Human Recombinant is a single polypeptide chain consisting of 222 amino acids (1-198) with a molecular weight of 24.7kDa. It features a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27495
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
DUSP18 Human
Dual Specificity Phosphatase 18 Human Recombinant
Recombinant human DUSP18, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 212 amino acids, with amino acids 1 through 188 forming the DUSP18 protein. The protein has a molecular weight of 23.6 kDa. For purification and further applications, a 24 amino acid His-tag is attached to the N-terminus of DUSP18. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27606
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
DUSP18 Human, Active
Dual Specificity Phosphatase 18 Human Recombinant, Active
Produced in E.Coli, DUSP18 is a single, non-glycosylated polypeptide chain comprising 212 amino acids (1-188a.a.) with a molecular weight of 23.6kDa. It features a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
DUSP19 Human
Dual Specificity Phosphatase 19 Human Recombinant
Recombinant human DUSP19, produced in E. coli, is a single polypeptide chain that lacks glycosylation. This protein consists of 176 amino acids (residues 65-217), resulting in a molecular weight of 19.4 kDa. For purification purposes, a 23 amino acid His-tag is attached to the N-terminus, enabling efficient purification via proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27766
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
FBP1 Human, Active
Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant
This product consists of the FBP1 enzyme, recombinantly produced in E. coli bacteria. It is a single polypeptide chain that lacks glycosylation and contains 358 amino acids (specifically, amino acids 1 to 338), resulting in a molecular weight of 39.0 kDa. For purification and detection purposes, the FBP1 protein has a 20 amino acid His-Tag attached to its N-terminus. The purification process utilizes proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT28972
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.
FBP2 Human
Fructose-1,6-Bisphosphatase 2 Human Recombinant
Recombinant human FBP2, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 39kDa. The protein consists of 362 amino acids, including a 23 amino acid His-tag at the N-terminus (amino acids 1-339). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29074
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
IMPA1 Human
Inositol Monophosphatase 1 Human Recombinant
Recombinant human IMPA1, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a His tag (20 amino acids) at its N-terminus. This protein consists of 297 amino acids (including the 20-amino acid His tag; the IMPA1 sequence spans from amino acid 1 to 277) and has a molecular weight of 32.3 kDa. The purification process for IMPA1 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29133
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
IMPA2 Human
Inositol Monophosphatase 2 Human Recombinant
Recombinant human IMPA2, fused with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain comprises 308 amino acids (residues 1-288) and has a molecular weight of 33.5 kDa. Purification of IMPA2 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
PHPT1 Human, Active
Phosphohistidine Phosphatase 1 Human Recombinant, Active
Produced in E. coli, PHPT1 is a single, non-glycosylated polypeptide chain consisting of 145 amino acids (1-125a.a.) and possesses a molecular mass of 15.9 kDa. This protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30033
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.
Introduction
Definition and Classification
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.
Biological Properties
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.
Biological Functions
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.
Modes of Action
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
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.
Applications
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 in the Life Cycle
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.
