Cayman PtdIns-(4,5)-P2 Binding Protein (GST-tagged)

Pleckstrin homology (pH) domains all contain a seven-standard b-sandwich that allows binding to various species of phosphatidylinositol (PtdIns) phosphates.¹ Most pH domains bind to PtdIns phosphates with weak affinity and low specificity. However, a small subclass binds specifically and with high-affinity for certain PtdIns phosphates. PtdIns-(4,5)-P₂ Binding Protein (GST-tagged) contains a highly specific pH domain that recognizes and binds PtdIns-(4,5)-P₂ (see Figure 1).² PtdIns phosphates represent a small percentage of total membrane phospholipids. However, they play a critical role in the generation and transmission of cellular signals.^3,4 PtdIns-(4,5)-P₂ can be phosphorylated by phosphoinositide (PI)-3-kinase to make PtdIns-(3,4,5)-P₃ which initiates an intricate signaling cascade that has been implicated in cancer⁵ PtdIns-(4,5)-P₂ binding protein can be used in in vitro assays for the detection of PtdIns-(4,5)-P₂ in PI3-kinase and PTEN phosphatase assays.

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