Purified anti-GRASP65

GRASP65 (golgi reassembly stacking protein 1, Golgi peripheral membrane protein p65, reassembly and stacking protein p65) is a 65 kD Golgi stacking protein. Alternatively spliced transcripts of GRASP65 have been identified. This protein is thought to play a role in establishing the stacked structure of the Golgi cisternae allowing sorting and modification of proteins exported from the endoplasmic reticulum. GRASP65 is cleaved by caspase-3 during apoptosis and can be partitioned by fragmentation and dispersal during entry into mitosis. GRASP65 is modified by phosphorylation (polo-like kinase-1 and cdc2-cyclin B). This protein has been shown to form a complex with the Golgi matrix protein GOLGA2; this complex then interacts with the vesicle docking protein p115,and tethering factor GM130.