Description
Key facts
Cell type:U-87 MG,
Species or organism:Human,
Tissue:Brain,
Form:LiquidSee storage information,
Knockout validation:Next Generation Sequencing,
Disease:Glioblastoma
Product details:
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-GSN, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Next Generation Sequencing, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Gelsolin is a multifunctional actin-binding protein that exists in two main isoforms: cytoplasmic and plasma. It has a molecular mass of approximately 82 kDa. Gelsolin is expressed in a wide range of tissues including muscle epithelial and nerve cells. The protein's main mechanical function involves severing actin filaments which helps to regulate actin polymerization and depolymerization. Researchers sometimes refer to gelsolin as 'GSN'. The presence of the protein helps maintain the dynamic organization of the cytoskeleton by interacting with actin filaments.
Biological function summary
This protein acts in cell movement apoptosis and signal transduction. Gelsolin contributes to the remodeling of the actin cytoskeleton by promoting the disassembly of actin filaments allowing cells to change shape and move. Although it operates independently gelsolin’s activity can be influenced by calcium ions and phosphoinositides leading to its participation in various cellular activities. Gelsolin plays a role in platelet activation and may regulate cellular responses through association with the cytoskeletal complex.
Pathways
Gelsolin participates in the regulation of the actin cytoskeleton and apoptotic pathways. Within these pathways gelsolin interacts with proteins like cofilin to modulate actin filament dynamics. In apoptotic pathways it collaborates by altering the cytoskeletal architecture impacting cell death mechanisms. Gelsolin modifications in these pathways have implications for cellular processes like cell migration and apoptosis bringing it into relation with proteins such as caspases.
Gelsolin is linked to conditions such as gelsolin amyloidosis and cancer metastasis. Gelsolin amyloidosis results from mutations in the gelsolin gene which lead to the formation of amyloid fibrils causing dysfunction in nerves eyes and skin. In cancer altered gelsolin expression can influence tumor progression and metastasis through its role in cell motility. Related proteins such as actin and caspases could also play a part in these conditions either through direct interaction or through pathways in which gelsolin functions.
