GM130. also known as Golgin subfamily A member 2 (GOLGA2), is a 130 kDa Golgi matrix protein encoded by the *GOLGA2* gene in humans. It is predominantly localized to the cis-Golgi network and plays a critical role in maintaining Golgi structure, vesicle trafficking, and glycosylation processes. GM130 interacts with other Golgi matrix proteins, such as GRASP65. to form the Golgi ribbon and ensure proper organelle stacking. Additionally, it participates in cell cycle regulation by contributing to Golgi disassembly and reassembly during mitosis.
GM130 antibodies are widely used tools in cell biology research to study Golgi morphology, dynamics, and functional disruptions. These antibodies, often raised in rabbits or mice, specifically recognize GM130 epitopes in techniques like immunofluorescence, Western blotting, and immunohistochemistry. Researchers rely on GM130 as a cis-Golgi marker to assess Golgi integrity in experimental models, including cancer, neurodegenerative diseases, and infectious diseases where Golgi fragmentation or dysfunction occurs. For example, altered GM130 expression has been linked to impaired protein trafficking in Alzheimer’s disease and disrupted cell division in certain cancers. When using GM130 antibodies, co-staining with other Golgi markers (e.g., TGN46 or Giantin) is recommended to validate subcellular localization and experimental outcomes.