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The GRIP family member, golgin 97, is a trans-Golgi network peripheral membrane protein with an extensive coiled-coil structure (67 % alpha-helical content) and a C-terminal GRIP domain. Golgin 97 localizes exclusively on the cytoplasmic face of the Golgi and can form homodimers. Binding of golgin 97 to the Golgi membrane is mediated by the G protein family member, Arl1. Golgin 97 acts as an essential player to the cell in the form of a tethering molecule associating with tubulovesicular carriers during the trafficking from the trans-Golgi network to the recycling endosome and/or early endosome. During poxvirus infection, golgin 97 accumulates at the site of viral replication and is incorporated into virions. It associates with the insoluble fraction of the virus core protein, playing a significant role in virus replication and maturation of the virus membrane and core protein. Golgin 97 takes on a rod-like shape and, although it seemingly lacks a transmembrane domain, it protrudes from the surface of the virion envelope.