Pleckstrin homology (PH) domains all contain a seven-standard β-sandwich that allows binding to various species of phosphatidyl inositol (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-(3,4,5)-P3 Binding Protein contains a highly specific PH domain that recognizes and binds PtdIns-(3,4,5)-P3 (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 signalling cascade that has been implicated in cancer.5 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.WARNING This product is not for human or veterinary use.
There are no reviews yet.