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Protein tyrosine phosphatases (PTPs) are a group of enzymes that catalyze the removal of phosphate groups from tyrosine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinase and phosphorylase enzymes.
|Cat No||Product Name / Activity|
|Selective inhibitor of PTPMT1|
|Non-competitive protein tyrosine phosphatase inhibitor; enhances insulin signaling|
|Selective CD45 inhibitor|
|Potent inhibitor of shp2 and shp1 PTP|
|PTPN2 and PTEN inhibitor|
|Protein tyrosine phosphatase inhibitor|
|Selective inhibitor of PTP1B|
|Potent PTEN inhibitor|
Protein tyrosine phosphatases (PTPs) are a group of enzymes that catalyze the removal of phosphate groups from tyrosine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinases and phosphorylases and therefore play an integral role in many signal transduction pathways, including histone dephosphorylation during epigenetic modification.
PTPs are cysteine-dependent phosphatases that contain a conserved C[X]5R motif essential for enzymatic activity. PTPs are currently divided into five subtypes: tyrosine-specific phosphatases (e.g. PTP1B); dual specificity phosphatases (DSPs) (e.g. DUSP1); Cdc25 phosphatases (e.g. Cdc25A); myotubularin-related phosphatases (e.g. MTMR13); and low molecular weight phosphatases (e.g. PTPase A). Perturbations in PTP activity have been implicated in human diseases, including type II diabetes. PTPs have been identified as a negative regulator of insulin signaling due to its ability to dephosphorylate phosphotyrosine residues of insulin receptor kinase. In cancers, PTPs dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation.
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|