GOLPH1 Antibody

GOLPH1 Antibody: GOLPH1, also known as GCP60, was initially identified as a Golgi protein that can interact with the integral membrane protein giantin and is thought to be involved in the maintenance of the Golgi structure. GOLPH1 has also been shown to interact with other Golgi proteins such as Golgin-160, a Golgi protein that can be cleaved by caspases-2, -3, and -7, leading to the nuclear localization of Golgin-160. GOLPH1 interaction with the Golgin-160 fragments is stronger than that with the intact Golgin-160, with its interaction regulated by the oxidation state of Cys-463 within GOLPH1, suggesting that the nuclear localization of the caspase-cleaved Golgin-160 fragments is a highly coordinated event. GOLPH1 has also been found to interact with Numb, a cytosolic signaling protein that mediates asymetric cell division of neural progenitor cells to a daughter progenitor cell and a neuron, suggesting that Golgi fragmentation and reconstitution during the cell cycle differentially regulate Numb signaling through changes in GOLPH1 subcellular distribution and may couple cell fate with cell cycle progression.

GOLPH1 antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Sohda M, Misumi Y, Yamamoto A, et al. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J. Biol. Chem.2001; 276:45298-306.

Mancini M, Machamer CE, Roy S, et al. Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J. Cell Biol.2000; 149:603-12.

Sbodio JI and Machamer CE. Identification of a redox-sensitive cysteine in GCP60 that regulates its interaction with Golgin-160. J. Biol. Chem.2007; 282:29874-81.

Zhou Y, Atkins JB, Rompani SB, et al. The mammalian Golgi regulates numb signaling in asymetric cell division by releasing ACBD3 during mitosis. Cell2007; 129:163-78.