|Detection of Human Supervillin by Western Blot. Western blot shows lysates of human thyroid tissue and human skeletal muscle tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Supervillin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7338) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). Specific bands were detected for Supervillin at approximately 240-250 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Supervillin ("Largest" villin [family member]; also Archvillin and p250) is a 240-250 kDa member of the villin/gelsolin family of proteins. It is expressed in select cell types, including platelets, neutrophils, renal epithelium and striated muscle cells. Supervillin is found intracellularly in both the nuclear and cytoplasmic compartments. Its principal function is to serve as a scaffold for molecules that interact to oversee changes in the actin cytoskeleton at the cell membrane. It is able to both crosslink F-actin and initiate actin bundle formation. It also binds nonmuscle myosin and negatively regulates focal adhesion complexes. Human supervillin is 2214 amino acids (aa) in length. It contains an NLS (aa 927-931), five gelsolin-like repeats that interact with F-actin (aa 1441-2122), and a C-terminal villin headpiece domain (aa 2179-2214). The 250 kDa form of supervillin (archvillin) is striated muscle-specific. There is also one general nonmuscle form of supervillin (p205) that is 200-210 kDa in size and contains two blocks of deletions between aa 276-669 and 749-781. In ferret, a third 220-230 kDa intermediate isoform has been reported that is unique to smooth muscle. Over aa 1801-2214, human supervillin shares 96% aa sequence identity with mouse supervillin.