|Application ||WB, IHC-P, FC, E|
|Other Accession||Q68FP1, P20305, P13020, Q3SX14|
|Predicted||Bovine, Pig, Rat|
|Calculated MW||85698 Da|
|Antigen Region||714-743 aa|
|Other Names||Gelsolin, AGEL, Actin-depolymerizing factor, ADF, Brevin, GSN|
|Target/Specificity||This GSN antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 714-743 amino acids from the C-terminal region of human GSN.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GSN Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.|
|Cellular Location||Isoform 2: Cytoplasm, cytoskeleton.|
|Tissue Location||Phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth and skeletal muscle cells|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
GSN binds to the 'plus' ends of actin monomers and filaments to prevent monomer exchange. The calcium-regulated protein functions in both assembly and disassembly of actin filaments. Defects in this protein are a cause of familial amyloidosis Finnish type (FAF).
Li,Q., Ye,Z. Biochem. Biophys. Res. Commun. 385 (2), 284-289 (2009) Walsh,N., Dowling,P. J Proteomics 71 (5), 561-571 (2008) Paunio,T., Kiuru,S. Genomics 13 (1), 237-239 (1992)
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