The GRASP65 antibody is a crucial tool in cellular biology research, specifically for studying the Golgi apparatus. GRASP65 (Golgi Reassembly Stacking Protein of 65 kDa) is a peripheral membrane protein localized to the *cis*-Golgi compartment. It plays a pivotal role in maintaining Golgi structure by mediating the stacking of cisternal membranes and facilitating Golgi ribbon formation. During mitosis, GRASP65 is phosphorylated, leading to Golgi disassembly, and its dephosphorylation post-mitosis aids in Golgi reassembly.
Researchers use GRASP65 antibodies primarily to investigate Golgi dynamics, vesicle trafficking, and organelle organization. These antibodies are widely applied in techniques like Western blotting (WB), immunofluorescence (IF), and immunoprecipitation (IP) to detect GRASP65 expression levels, subcellular localization, and interactions with other proteins (e.g., golgins or Rab GTPases).
The antibody’s specificity varies depending on the clone and host species (commonly rabbit or mouse). Polyclonal antibodies offer broad epitope recognition, while monoclonal versions provide higher reproducibility. Validated GRASP65 antibodies help explore pathological conditions linked to Golgi dysfunction, such as cancer metastasis, neurodegenerative diseases (e.g., Alzheimer’s), and secretion disorders.
Recent studies also utilize GRASP65 antibodies to dissect unconventional protein secretion pathways or autophagy-related processes. Proper controls (e.g., knockout cell lines) are essential to confirm antibody specificity, given potential cross-reactivity with paralogs like GRASP55. Overall, GRASP65 antibodies remain indispensable for unraveling Golgi-related mechanisms in health and disease.