Golgin 97 Recombinant Rabbit mAb (S-6031)

Golgin 97 (Golgi protein 97) is a peripheral membrane protein belonging to the golgin family of Golgi matrix proteins, localized to the trans-face of the Golgi apparatus. Its C-terminus anchors to the Golgi membrane via a transmembrane domain or through interactions with GRASP proteins, while its N-terminus extends into the cytoplasm, forming a long coiled-coil structure that acts as a "scaffold" to maintain the stacked flattened membrane sacs (cisternae) of the Golgi in an ordered lamellar arrangement. However, it is by no means merely a structural protein; it plays a central "hub" role in intracellular vesicular transport—through interactions with various transport-related proteins (such as Rab GTPases, SNARE proteins, and dynein complexes), it functions as a tethering factor that captures and guides transport vesicles derived from endosomes or the trans-Golgi network to precisely fuse with the trans-Golgi membranes, thereby finely regulating the sorting and transport of specific cargo proteins. In recent years, non-canonical functions of Golgin 97 in tumor biology and infectious immunity have also garnered significant attention: for example, it is "hijacked" by certain intracellular pathogens such as Salmonella, participating in the recruitment of their effector proteins to help the bacteria evade host immune defenses; meanwhile, altered expression of Golgin 97 in tumors such as colorectal cancer has also been associated with tumor cell migration capacity, positioning it as a potential disease target or biomarker.