PPP1R1A Human

Protein Phosphatase Inhibitor-1 Human Recombinant

Recombinant human PPP1R1A, expressed in E. coli with a C-terminal His tag, is a single, non-glycosylated polypeptide chain. It comprises 179 amino acids, resulting in a molecular weight of 20 kDa. The purification of PPP1R1A is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT547
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PPP1R2 Human

Protein Phosphatase 1, Regulatory Subunit 2 Human Recombinant

Recombinant Human PPP1R2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 189 amino acids (with amino acids 1-166 comprising the PPP1R2 sequence) and has a molecular weight of 21kDa. The recombinant protein includes a 23 amino acid His-tag fused to the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT635
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless, and clear solution.

PSPH Human

Phosphoserine Phosphatase Human Recombinant

Recombinant Human Phosphoserine Phosphatase, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 225 amino acids. It has a molecular weight of 25 kDa. The production process involves overexpression in E. coli followed by purification using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1182
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

RNGTT Human

RNA Guanylyltransferase And 5'-Phosphatase Human Recombinant

Recombinant human RNGTT, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 620 amino acids (1-597a.a). It has a molecular weight of 70.9 kDa. This RNGTT protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1229
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

SSU72 Human

SSU72 RNA Polymerase II CTD Phosphatase Human Recombinant

Recombinantly produced in E. coli, the human SSU72 protein is a single, non-glycosylated polypeptide chain comprising 217 amino acids (specifically residues 1-194). With a molecular weight of 25.0 kDa, this SSU72 variant is characterized by a 23 amino acid His-tag fused at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1337
Source
E.coli.
Appearance
A clear, sterile solution without any color.

THTPA Human

Thiamine Triphosphatase Human Recombinant

Recombinant Human THTPA, produced in E.Coli, is a single, non-glycosylated polypeptide chain composed of 250 amino acids (specifically, amino acids 1 to 230). It has a molecular weight of 27.7 kDa. A 20 amino acid His-Tag is fused to the N-Terminus of the THTPA. Purification is achieved using standard chromatography methods.
Shipped with Ice Packs
Cat. No.
BT1410
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PPM1G Human, 546 a.a.

Protein Phosphatase 1G 546 a.a. Human Recombinant

Recombinant PPM1G Human, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 566 amino acids (1-546). It has a molecular weight of 61.4 kDa. The PPM1G protein is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT173
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

PPP1CA Human

Protein Phosphatase 1, Catalytic Subunit Alpha Human Recombinant

Recombinant human PPP1CA, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 350 amino acids (residues 1-330) with a molecular weight of 39.7 kDa. This protein contains a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT253
Source
Escherichia Coli.
Appearance
A clear, yellowish solution, sterile-filtered.

PPP1CC Human

Protein Phosphatase 1, Catalytic Subunit Gamma Human Recombinant

Recombinant human PPP1CC, produced in E. coli, is a single polypeptide chain consisting of 343 amino acids (residues 1-323) with a molecular weight of 39.1 kDa. This protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT319
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

PPP1CC Human, Active

Protein Phosphatase 1, Catalytic Subunit Gamma Human Recombinant, Active

Produced in E. coli, our PPP1CC protein is a single, non-glycosylated polypeptide chain. It consists of 343 amino acids (1-323a.a.) with a molecular weight of 39.1 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.
BT385
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.
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.
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