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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|
|Competitive PTP1B inhibitor|
|Selective CD45 inhibitor|
|Potent inhibitor of shp2 and shp1 PTP|
|6771||PHPS1 sodium salt|
|Shp2 (PTPN11) inhibitor|
|PTPN2 and PTEN inhibitor|
|PTEN inhibitor; induces necroptosis; anti-inflammatory|
|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. In cancers, PTPs dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation.
Tocris offers the following scientific literature for Protein Tyrosine Phosphatases to showcase our products. We invite you to request* or download your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|