Anti-Giantin antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Giantin also known as Giantin Golgi or Giantin protein is a large coiled-coil protein with a molecular mass of approximately 376 kDa. It localizes primarily to the cis/medial region of the Golgi apparatus serving as a Golgi marker. As a part of the structural framework of the Golgi it plays an important role in maintaining the integrity and architecture of the Golgi stacks. Giantin is highly expressed in a variety of cell types including those in the liver kidney and brain making it an important target in cell biology studies.

Biological function summary

The Giantin protein functions as a scaffold that supports the Golgi apparatus’s dynamic organization. It is part of a larger complex that influences vesicular trafficking within the cell. This ability to interact with various vesicle coat proteins points to its important role in the sorting and transport of proteins and lipids through the secretory pathway. Besides Giantin is involved in the assembly of the Golgi matrix and influences its disassembly during mitosis suggesting a significant involvement in cell proliferation and division.

Pathways

Giantin helps regulate intracellular transport pathways connecting the endoplasmic reticulum (ER) and Golgi as well as intra-Golgi trafficking. It interfaces with other significant proteins such as GM130 and GRASP65 which are involved in Golgi dynamics and structure. This protein also participates in the coordination of the secretory pathway important for the modification and sorting of proteins destined for the cell surface or lysosomes.

Associated diseases and disorders

Giantin has been linked to conditions involving impaired protein glycosylation and Golgi-related transport defects. Notably defects in Giantin function are associated with connective tissue disorders and certain forms of Golgi dysfunctions like Congenital Disorders of Glycosylation (CDG). Additionally Giantin’s interactions with proteins such as Sec23/24 and Bet3 which are cargo-binding components of the COPII vesicle coat connect its functional disruption to diseases characterized by impaired vesicular trafficking and cellular secretion malfunctions.