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Product List
PTP4A1 Human
Protein Tyrosine Phosphatase Type IVA Member 1 Human Recombinant
PTP4A1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (1-170 a.a.) and having a molecular mass of 21.6kDa. The PTP4A1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT25418
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
PTP4A2 Human
Protein Tyrosine Phosphatase Type IVA Member 2 Human Recombinant
Recombinant Human PTP4A2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-167 a.a.) and having a molecular mass of 23.2 kDa. PTP4A2 is fused to a 36 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT25497
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
PTP4A3 Human
Protein Tyrosine Phosphatase Type IVA Member 3 Human Recombinant
PTP4A3 Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 193 amino acids (1-173 a.a.) and having a molecular mass of 21.6kDa.
The PTP4A3 is purified by proprietary chromatographic techniques.
The PTP4A3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25589
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
PTPMT1 Human
Protein Tyrosine Phosphatase, Mitochondrial 1 Human Recombinant
PTPMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (28-201) and having a molecular mass of 22.6kDa.
PTPMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PTPMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25663
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
PTPN1 Human
Protein Tyrosine Phosphatase Non Receptor Type-1 Human Recombinant
Protein Tyrosine Phosphatase Non Receptor Type-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 321 amino acids and having a molecular mass of 37.3 kDa.
Shipped with Ice Packs
Cat. No.
BT25733
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
PTPN11 Human
Protein Tyrosine Phosphatase Non Receptor Type-11 Human Recombinant
PTPN11 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 469 amino acids (1-460a.a.) and having a molecular mass of 53.9kDa. PTPN11 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25828
Source
Sf9,
Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
PTPN4 Human
Protein Tyrosine Phosphatase Non Receptor Type-4 Human Recombinant
PTPN4 Human Recombinant produced in E.Coli is a single, non-glycosylated
polypeptide chain containing 280 amino acids (655-913 a.a) and having a
molecular mass of 32kDa.
PTPN4 is fused to a 21 amino acid His-tag at N-terminus
& purified by proprietary chromatographic techniques.
Shipped with Ice Packs
PTPN6 Human
Protein Tyrosine Phosphatase Non Receptor Type-6 Human Recombinant
PTPN6 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 300 amino acids and having a molecular mass of 34.3 kDa. The protein coding region of the catalytic domain of PTPN6 (amino acids 243-541). The catalytic domain of PTPN6 was overexpressed as insoluble protein aggregates (inclusion bodies). The recombinant PTPN6 protein was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. Additional amino acid(Met) is attached at N-terminus.
Shipped with Ice Packs
Cat. No.
BT26002
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
PTPN7 Human
Protein Tyrosine Phosphatase Non Receptor Type-7 Human Recombinant
PTPN7 Human Recombinant produced in E. coli is a single polypeptide chain containing 384 amino acids (1-360) and having a molecular mass of 43.1kDa.
PTPN7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PTPN7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
PTPRC Human
Protein Tyrosine Phosphatase Receptor Type C Human Recombinant
PTPRC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (1031-1251a.a) and having a molecular mass of 29.6kDa.
PTPRC is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PTPRC is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26171
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Introduction
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.
