Cayman PtdIns-(3,4,5)-P3 Binding Protein

Pleckstrin homology (pH) domains all contain a seven-standard β-sandwich that allows binding to various species of phosphatidyl inositol (PtdIns) phosphates. 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-(3,4,5)-P₃ Binding Protein contains a highly specific pH domain that recognizes and binds PtdIns-(3,4,5)-P₃ (see Figure 1). PtdIns phosphates represent a small percentage of total membrane phospholipids. However, they play a critical role in the generation and transmission of cellular signals.^, PtdIns-(4,5)-P₂ can be phosphorylated by phosphoinositide (PI)-3-kinase to make PtdIns-(3,4,5)-P₃ which initiates an intricate signalling cascade that has been implicated in cancer. Due to PtdIns-(3,4,5)-P₃ binding protein · s unique affinity for PtdIns-(3,4,5)-P₃, this protein can be used to detect product formed by PI3-kinase in in vitro assays. Cayman’s PtdIns-(3,4,5)-P₃ Binding Protein is isoform 2, which differs from isoform 1 by the absence of a glycine residue at position 277.

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