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Product List
PGP Human
Phosphoglycolate Phosphatase Human Recombinant
Produced in E. coli, our PGP protein is a non-glycosylated polypeptide chain consisting of 345 amino acids (with the active protein encompassing amino acids 1 to 321). It possesses a molecular weight of 36.5 kDa. For purification purposes, a 24 amino acid His-tag is fused to the N-terminus, and the protein undergoes rigorous purification using proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT29723
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
PGP Human, Active
Phosphoglycolate Phosphatase Human Recombinant, Active
Recombinant human PGP, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 345 amino acids (1-321a.a) with a molecular weight of 36.5 kDa. It includes a 24-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29791
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
DUSP22 Human
Dual Specificity Phosphatase 22 Human Recombinant
Recombinant DUSP22, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain. This chain consists of 207 amino acids (specifically, amino acids 1 through 184) and has a molecular mass of 23.3 kDa. The DUSP22 is fused to a 23 amino acid His-tag located at the N-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27930
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized through filtration.
DUSP23 Human
Dual Specificity Phosphatase 23 Human Recombinant
Recombinant human DUSP23, a non-glycosylated polypeptide, is produced in E. coli. This 18.8 kDa protein consists of 170 amino acids, including a 20 amino acid His-tag fused at the N-terminus (1-150 a.a. of DUSP23). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28026
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
DUSP23 Human, Active
Dual Specificity Phosphatase 23 Human Recombinant, Active
DUSP23 Human Recombinant, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 170 amino acids (specifically, amino acids 1 to 150). It possesses a molecular mass of 18.8 kDa. A 20 amino acid His-tag is fused to the N-terminus of DUSP23. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28103
Source
Escherichia Coli.
Appearance
Clear solution, sterile, and filtered.
DUSP26 Human
Dual Specificity Phosphatase 26 Human Recombinant
This product consists of the human DUSP26 protein, recombinantly produced in E. coli bacteria. This protein is not glycosylated, meaning it lacks attached sugar molecules. It is a single polypeptide chain comprising 234 amino acids, with amino acids 1 to 211 constituting the DUSP26 sequence. A 23-amino acid His-tag is attached to the protein's N-terminus for purification purposes. The molecular weight of the protein is 26.3 kDa. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT28176
Source
Escherichia Coli.
Appearance
A clear solution free from any particles or cloudiness.
FBP1 Human
Fructose-1,6-Bisphosphatase 1 Human Recombinant
This recombinant human FBP1 protein, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 39kDa. Comprising 358 amino acids (1-338 a.a.), the enzyme features a 20 amino acid His-Tag at its N-terminus. Purification is achieved through proprietary chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28869
Source
Escherichia Coli.
Appearance
Clear solution, sterile and filtered.
ITPA Human
Inosine Triphosphatase Human Recombinant
ITPA Recombinant Human, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 215 amino acids (specifically, amino acids 1 to 194). It possesses a molecular weight of 23.7 kDa. For purification and identification purposes, a 21 amino acid His-Tag is attached to the N-terminus of the ITPA protein. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29266
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.
LHPP Human
Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant
Recombinant human LHPP, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 307 amino acids, with amino acids 1-270 representing the LHPP protein, and has a molecular weight of 33.5 kDa. A 37 amino acid His-tag is fused to the N-terminus of the protein to facilitate purification, which is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29327
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.
MDP1 Human
Magnesium-Dependent Phosphatase 1 Human Recombinant
Recombinant human MDP1, expressed in E. coli, is a non-glycosylated polypeptide chain with a His tag (24 amino acids) at the N-terminus. This protein consists of 200 amino acids (including the His tag, residues 1-176 represent MDP1) and has a molecular weight of 22.6 kDa. Purification of MDP1 is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29410
Source
Escherichia Coli.
Appearance
A clear and colorless solution, sterilized by 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.
