525189 Sigma-AldrichPhospholipase C-γ-2, His•Tag^®, Human, Recombinant, S. frugiperda

This product has been discontinued.

Full-length, recombinant, human phospholipase C γ-2 fused at the N-terminus to His•Tag^® and S•Tag™ sequences and expressed in S. frugiperda insect cells. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Intrinsic enzyme activity has not been tested. Production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes, which are crucial enzymes in transmembrane signaling. PLC-γ-2 is phosphorylated on tyrosine residues following ligand-induced activation of a variety of growth factor receptors and immune system receptors, resulting in increased phospholipase activity. The full-length proteins contains the following domains: C2 domain (aa 1059-1152); PH domain (aa 20-131); PI-PLC X-box catalytic domain (aa 312-456); PI-PLC Y-box catalytic domain (aa 930-1044); two SH2 domains (aa 532-635, aa 646-735); and a SH3 domain (aa 769-829). It has been reported to be phosphorylated at Tyr⁷⁵³ and Tyr⁷⁵⁹ (Btk, Src, Fyn, Lck), and Tyr¹²¹⁷ and Tyr¹²⁴⁵ by Bcr-Abl.