The Golgi apparatus is a critical cell organelle involved in protein processing, sorting, and transport within eukaryotic cells. Golgi proteins play essential roles in maintaining Golgi structure and function, as well as participating in various cellular processes, including in cell signalling. Golgi proteins are primarily localized to different subcompartments of the Golgi apparatus, including the cis-Golgi, medial-Golgi, and trans-Golgi. Specific targeting signals, such as transmembrane domains and protein-protein interaction domains, facilitate their proper localization within the Golgi. Golgi proteins are involved in the sorting and modification of proteins passing through the Golgi. For example, they facilitate post-translational modifications, including glycosylation, phosphorylation, and sulfation, which are crucial for protein functionality and recognition. Golgi-resident enzymes, such as glycosyltransferases, are responsible for catalysing these protein modifications. Golgi proteins also participate in the formation of transport vesicles that mediate the trafficking of proteins and lipids to their target destinations. They interact with coat proteins, such as clathrin and COPI/COPII, to facilitate vesicle budding and cargo selection. Golgi-localized proteins, such as golgins, are involved in maintaining Golgi structure and regulating vesicle trafficking. Golgi proteins also play a critical role in sorting and directing proteins to their appropriate secretion pathways. They ensure the correct trafficking of signalling molecules, including growth factors, cytokines, and hormones, to their target locations. For example, the Golgi protein furin is involved in the processing and activation of several growth factors and receptors, in addition to viral proteins such as the SARS-CoV-2 spike protein. Golgi proteins also mediate glycosylation, a process that adds sugar moieties to proteins, thereby influencing cell-cell interactions and signal recognition. Glycosylation plays a vital role in modulating the activity, stability, and cellular localization of many cell surface receptors and adhesion molecules. Notable examples include the Golgi-resident enzyme N-acetylglucosaminyltransferase V (GnT-V), which modifies integrins, influencing cell adhesion and cell migration. The Golgi apparatus generates specific vesicles that participate in cell signalling. For instance, exosomes, which are small membrane-bound vesicles derived from the Golgi, are involved in intercellular communication by transferring bioactive molecules, including proteins and nucleic acids, to target cells. Exosomes are now thought to influence various cellular processes, such as immune response modulation and tumour progression. Finally, Golgi proteins contribute to lipid metabolism and the regulation of lipid-mediated signalling pathways. They are involved in lipid synthesis, transport, and sorting, which are crucial for maintaining proper membrane composition and lipid-mediated signalling events. Golgi-localized enzymes, such as phospholipase D, also play a role in generating lipid second messengers that modulate cellular processes, including cell growth and vesicle trafficking. We offer a wide product catalogue of research tools for investigating golgi proteins, including M6PR (cation independent) antibodies, GLG1 antibodies, p40 antibodies, ARF4 antibodies, and Perilipin 3 antibodies. Explore our full golgi proteins product range below and discover more, for less.