GRASP抗体;GRASP Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human lung cancer tissue using P13457(GRASP Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P13457(GRASP Antibody) at dilution 1/60. (Original magnification: ×200)    

  
  

GRASP (Golgi ReAssembly Stacking Protein) antibodies are tools used to study the GRASP family of proteins, which play critical roles in Golgi apparatus structure and function. First identified in the early 2000s, GRASP proteins (GRASP55 and GRASP65 in mammals) are peripherally associated with Golgi membranes and are essential for maintaining its stacked cisternal architecture. They facilitate the tethering of incoming vesicles and mediate Golgi reassembly after mitosis or fragmentation during cellular stress. GRASP65 localizes to the cis-Golgi, while GRASP55 is found in the medial/trans regions, reflecting their distinct yet cooperative roles in membrane stacking and trafficking.

Antibodies targeting GRASP proteins are widely used in research to investigate Golgi dynamics, particularly during cell division, secretion, and stress responses. Studies using these antibodies have revealed GRASP's involvement in unconventional protein secretion pathways, where they bypass the classical ER-Golgi route, such as in the secretion of inflammatory cytokines like IL-1β. Dysregulation of GRASP proteins has been linked to diseases, including neurodegenerative disorders and cancers, where altered Golgi structure correlates with pathological secretion or signaling.

Recent work also highlights GRASP's non-canonical roles in autophagy, apoptosis, and cell adhesion, expanding its relevance beyond Golgi maintenance. GRASP antibodies thus serve as vital reagents for dissecting Golgi-related mechanisms in health and disease.