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Maturation and post-translational modification of proteins occurs after their biosynthesis at the endoplasmic reticulum and their transport through the Golgi apparatus. The process involves the transport of vesicles carrying the proteins through a vectorial process of vesicle budding and fusion from the cis-compartment to the medial-compartment and the trans-compartment of the Golgi apparatus. The detergent insoluble fraction of the Golgi is named “matrix” and is required for proper morphology of the Golgi membranes. GM130 (Golgi matrix protein of 130kDa) is a protein isolated from the Triton™ X-100-insoluble Golgi matrix and peripherally associated with the cis compartment, as demonstrated by co-localization with syntaxin5. GM130 is homologous to the Golgi autoantigen golgin 95. GM130 interacts through its N-terminal domain with p115 and with the Golgi membranes at the C-terminal portion. Furthermore, the mitotic phosphorylation of GM130 blocks the interaction with p115. Thus, GM130 appears to function as a structural element of the Golgi apparatus that also provides attachment sites for membranes and other Golgi proteins. The 35/GM130 monoclonal antibody recognizes GM130, regardless of phosphorylation status.Host Species: MouseClone: 35Isotype: IgG1Species Reactivity [for Features Main]: HumanImmunogen: Rat GM130 aa. 869-982Immunofluorescence, Immunoprecipitatio
