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Item No. 10009815
![PtdIns-(4,5)-P2 Binding Protein (GST-tagged) (Phosphatidylinositol-4,5-diphosphate, PI(4,5)-P2, PI(4,5)P2 Binding Protein, PIP2, PIP2[4',5'] Binding Protein, PLC-δ1-PH Domain)](https://cdn2.caymanchem.com/cdn/productImages/10009815.png)
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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)-
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1. Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides. Biochem. Soc. Trans. 29(4), 377-384 (2001).
2. Phosphoinositide recognition domains. Traffic 4(4), 201-213 (2003).
3. Regulation of phosphoinositide phospholipases by hormones, neurotransmitters, and other agonists linked to G proteins. Annu. Rev. Pharmacol. Toxicol. 36, 481-509 (1996).
4. The phosphatidylinositol 3-