Villin is a member of a conserved family of actin-associated proteins, such as gelsolin, adseverin, and scinderin, widely expressed from slime molds to humans. These proteins belong to the group of actin-severing proteins that contain 3–6 repeats of a conserved domain. Similar to other family members, villin caps, nucleates, and severs actin filaments, and these functions are confined to the villin repeats (S1–S6). In addition, villin contains a carboxyl-terminal domain (S7) called the headpiece, which provides villin the ability to cross-link actin filaments. Villin is tyrosine-phosphorylated in vitro and in vivo by c-Src kinase similar to gelsolin, fragmin, and CapG. Villin is phosphorylated at multiple tyrosine sites in the N-terminal and C-terminal domains. Tyrosine phosphorylation of villin releases its auto-inhibited conformation allowing it to sever actin at physiologically relevant calcium concentrations, and induce changes in cell shape and cell motility.
Tomar, A. et al. (2006) J. Biol. Chem. 281(42):31972.
Tomar, A. et al. (2004) Mol. Biol. Cell 15:4807.
Clone (M245) was generated from a recombinant full length human villin protein. This sequence is conserved in rat and mouse villins.
Western blot analysis of adult mouse kidney. The blot was probed with mouse monoclonal anti-Villin-1 (VM2451) at 1:250.
*For more information, see UniProt Accession P09327
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
The antibody detects a 95 kDa* protein corresponding to villin on SDS-PAGE immunoblots of mouse kidney.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot
mobilities of known proteins with similar MW.