Formins contain a conserved formin homology 2 (FH2) domain that is essential for dimerization and subsequent actin filament assembly. N-terminal to this domain is the formin homology 1 (FH1) domain that functions in the physiological action of formins by recruiting profilin-bound actin monomers to the growing actin filament. FMNL1 contains a GTPase binding domain (GBD) and a diaphanous autoregulatory domain (DAD), additionally.
Synonyms: Anti-CLL-associated antigen KW-13; Anti-Formin-like protein 1; Anti-Leukocyte formin
Storage: -20C
Application: Anti-FMNL1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org). Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: FMNL1 (formin-like 1) gene encodes a leukocyte formin that has been found to be overexpressed in lymphomas. FMNL1 is a member of the diaphanous-related formins (DRFs) that are activated by Rho GTPase binding to the GBD (GTPase binding domain). Formins are large multi-domain proteins that function in the polymerization of unbranched actin filaments and regulate cytoskeletal dynamics. They also function in the maintenance of cell polarity, adhesion and migration. The Rho GTPases, Rac1 and RhoA, are involved in the binding and activation of FMNL1.
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