Golgi Matrix Protein (GM130) is a peripheral cytoplasmic protein that is bound to Golgi membranes. It maintains cis-Golgi structure, and it regulates the disassembly and reassembly of the Golgi complex during mitosis. GM130 may also be important during docking and fusion of coatomer (COPI) coated vesicles to the Golgi membrane. The carboxy-terminal domain of GM130 is highly homologous to the human auto-antigen, golgin-95. GM130 interacts in a GTP-dependent manner with Rab1b protein, a regulator of anterograde traffic between ER and Golgi membranes. It has also been implicated in the activation of Ste-kinase, YSK1, during the golgi reorganization that occurs along with cell migration.
Nakamura, N. et al. (1995) J Cell Biol 131:1715.
Warren, G. (1993) Annual Rev Biochem 62:323.
*For more information, see UniProt Accession Q08379
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Lin, Q. et al. (2017) J Cell Sci. 130(22):3839. (ICC: human A549 cells)
Sun, A. et al. (2017) Autophagy. 13(3):522. (ICC: human A549 cells)
Vazquez-Calvo, A. et al. (2016) Front Microbiol. 7:612. (WB: bovine kideny cells)
Martín-Acebes, M.A. et al. (2014) J virology 88(20): 12041. (ICC: human HeLa cells)
Mart?n-Acebes, M.A. et al. (2011) PLoS ONE 6(9): e24970. (ICC: monkey Vero cell)
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