PTPN7 Human

Protein Tyrosine Phosphatase Non Receptor Type-7 Human Recombinant

Recombinant human PTPN7 protein was expressed in E. coli and purified to a single polypeptide chain containing 384 amino acids (residues 1-360) with a molecular weight of 43.1 kDa. The protein consists of a 24 amino acid His-tag fused at the N-terminus and was purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26073
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

PTPRC Human

Protein Tyrosine Phosphatase Receptor Type C Human Recombinant

Recombinant human PTPRC, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 257 amino acids (1031-1251a.a). With a molecular weight of 29.6kDa, it features a 36 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26171
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PTPN1 Human

Protein Tyrosine Phosphatase Non Receptor Type-1 Human Recombinant

This product consists of the human recombinant Protein Tyrosine Phosphatase Non-Receptor Type 1, produced in E. coli. This single, non-glycosylated polypeptide chain comprises 321 amino acids, resulting in a molecular weight of 37.3 kDa.
Shipped with Ice Packs
Cat. No.
BT25733
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

PTPN11 Human

Protein Tyrosine Phosphatase Non Receptor Type-11 Human Recombinant

PTPN11, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 469 amino acids (specifically, amino acids 1 to 460a.a.). It has a molecular weight of 53.9 kDa. The protein is engineered with a 6-amino acid His tag located at the C-terminus to facilitate purification, which is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25828
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

PTPN4 Human

Protein Tyrosine Phosphatase Non Receptor Type-4 Human Recombinant

Recombinant human PTPN4 protein, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 280 amino acids (residues 655-913). It has a molecular weight of 32 kDa. The protein includes a 21 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25901
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PTPN6 Human

Protein Tyrosine Phosphatase Non Receptor Type-6 Human Recombinant

Recombinant human PTPN6, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 300 amino acids. It encompasses the catalytic domain of PTPN6 (amino acids 243-541) and has a molecular weight of 34.3 kDa. The catalytic domain was overexpressed in E. coli as insoluble protein aggregates (inclusion bodies). After refolding the isolated inclusion bodies in a redox buffer, recombinant PTPN6 was purified using FPLC gel-filtration chromatography. An additional methionine residue is present at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT26002
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PTP4A1 Human

Protein Tyrosine Phosphatase Type IVA Member 1 Human Recombinant

Recombinant human PTP4A1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 190 amino acids (1-170 a.a.) with an N-terminal 20 amino acid His tag. This protein, with a molecular weight of 21.6 kDa, is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25418
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

PTP4A2 Human

Protein Tyrosine Phosphatase Type IVA Member 2 Human Recombinant

Recombinant Human PTP4A2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 203 amino acids (residues 1-167) and exhibiting a molecular weight of 23.2 kDa. The protein is fused to a 36-amino acid His-Tag at its N-terminus and purified using standard chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25497
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PTP4A3 Human

Protein Tyrosine Phosphatase Type IVA Member 3 Human Recombinant

Recombinant human PTP4A3, expressed in E. coli, is a non-glycosylated polypeptide chain containing 193 amino acids (with an N-terminal 20 amino acid His tag). It has a molecular weight of 21.6 kDa. The protein is purified using proprietary chromatographic methods and is supplied in a non-glycosylated form.
Shipped with Ice Packs
Cat. No.
BT25589
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PTPMT1 Human

Protein Tyrosine Phosphatase, Mitochondrial 1 Human Recombinant

Recombinant PTPMT1, derived from humans and expressed in E. coli, is a non-glycosylated polypeptide consisting of 199 amino acids (residues 28-201). It has a molecular weight of 22.6 kDa. This PTPMT1 protein includes a 25 amino acid His-tag at the N-terminus to facilitate purification by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25663
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.
Definition and Classification

Protein Tyrosine Phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. This dephosphorylation process is crucial for regulating various cellular functions. PTPs are classified into several families based on their structure and function, including:

  • Classical PTPs: These are further divided into receptor-like PTPs (RPTPs) and non-receptor PTPs (NRPTPs).
  • Dual-specificity phosphatases (DUSPs): These can dephosphorylate both tyrosine and serine/threonine residues.
  • Low molecular weight PTPs (LMW-PTPs): These are smaller in size and have distinct structural features.
Biological Properties

Key Biological Properties:

  • Catalytic Activity: PTPs catalyze the hydrolysis of phosphate groups from tyrosine residues.
  • Substrate Specificity: They exhibit high specificity for phosphorylated tyrosine residues.

Expression Patterns:

  • PTPs are ubiquitously expressed in various tissues, with specific isoforms showing tissue-specific expression patterns.

Tissue Distribution:

  • Receptor-like PTPs: Predominantly found in the nervous system and immune cells.
  • Non-receptor PTPs: Widely distributed across different tissues, including liver, kidney, and muscle.
Biological Functions

Primary Biological Functions:

  • Signal Transduction: PTPs play a critical role in cellular signaling by modulating the phosphorylation status of key signaling molecules.
  • Cell Growth and Differentiation: They regulate processes such as cell proliferation, differentiation, and apoptosis.

Role in Immune Responses:

  • PTPs are involved in the activation and regulation of immune cells, including T cells and B cells.
  • They modulate the signaling pathways that control immune responses and pathogen recognition.
Modes of Action

Mechanisms with Other Molecules and Cells:

  • PTPs interact with various proteins, including kinases, receptors, and scaffolding proteins, to regulate signaling pathways.

Binding Partners:

  • PTPs have specific binding partners, such as SH2 domain-containing proteins, which help in targeting and regulating their activity.

Downstream Signaling Cascades:

  • PTPs influence downstream signaling cascades, including the MAPK, PI3K/Akt, and JAK/STAT pathways, by dephosphorylating key signaling molecules.
Regulatory Mechanisms

Regulatory Mechanisms:

  • Transcriptional Regulation: The expression of PTP genes is regulated by various transcription factors and signaling pathways.
  • Post-translational Modifications: PTPs undergo modifications such as phosphorylation, ubiquitination, and oxidation, which modulate their activity and stability.
Applications

Biomedical Research:

  • PTPs are studied for their role in various diseases, including cancer, diabetes, and autoimmune disorders.

Diagnostic Tools:

  • PTPs serve as biomarkers for certain diseases, aiding in diagnosis and prognosis.

Therapeutic Strategies:

  • Targeting PTPs with specific inhibitors or activators is being explored as a potential therapeutic approach for treating various diseases.
Role in the Life Cycle

Role Throughout the Life Cycle:

  • Development: PTPs are essential for embryonic development and organogenesis.
  • Aging: Changes in PTP activity are associated with aging and age-related diseases.
  • Disease: Dysregulation of PTPs is linked to the pathogenesis of various diseases, including cancer, neurodegenerative disorders, and metabolic diseases.
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