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MCE 国际站:Phosphatase Inhibitor Library
Protein phosphorylation is a key post-translational modification underlying the regulation of many cellular processes. Phosphatases and kinases contribute to the regulation of protein phosphorylation homeostasis in the cell. This reversible regulation of protein phosphorylation is critical for the proper control of a wide range of cellular activities, including cell cycle, proliferation and differentiation, metabolism, cell-cell interactions, etc.Protein phosphatases have evolved in separate families that are structurally and mechanistically distinct. Based on substrate specificity and functional diversity, protein phosphatases are classified into two superfamilies: Protein serine/threonine phosphatases and Protein tyrosine phosphatases. Ser/Thr phosphatases are metalloenzymes belonging to two major gene families termed PPP (phosphoprotein phosphatase) and PPM (metal-dependent protein phosphatases), whereas protein tyrosine phosphatases (PTPs) belong to distinct classes of enzymes that utilize a phospho-cysteine enzyme intermediate as a part of their catalytic action.MCE supplies a unique collection of 119 phosphatase inhibitors that mainly targeting protein tyrosine phosphatases (PTPs) and serine/threonine-specific protein phosphatases. MCE Phosphatase Inhibitor Library is a useful tool for phosphatase drug discovery and related research.
Description & Advantages:
• A unique collection of 119 phosphatase inhibitors for high throughput screening (HTS) and high content screening (HCS).
• The library contains compounds targeting protein tyrosine phosphatases (PTPs) and serine/threonine-specific protein phosphatases (PP1, PP2A, and PP2B, etc.).
• Bioactivity and safety confirmed by preclinical research and clinical trials. Some inhibitors have been approved by FDA.
• Structurally diverse, medicinally active, and cell permeable.
• Rich documentation with structure, IC50, and customer reviews.
• NMR and HPLC validated to ensure high purity.
• All compounds are in stock and continuously updated.