The Tagln gene encodes a shape-change and transformation-sensitive actin-binding protein. It's widely expressed in vascular and visceral smooth muscle, and it serves as an early marker of smooth muscle differentiation. The encoded protein is believed to be involved in calcium-independent smooth muscle contraction. It acts as a tumor suppressor, and a loss of its expression is an early event in cell transformation and the development of certain tumors, consistent with cellular plasticity. The encoded protein has a domain structure consisting of an N-terminal calponin-homology (CH) domain and a C-terminal calponin-like (CLIK) domain. Mice with a knockout of the homologous gene are viable and fertile, but their vascular smooth muscle cells show altered actin filament distribution and changes in cytoskeletal organization. Diseases associated with TAGLN include Peyronie's disease and Werner syndrome. Its related pathways include the PDGFR signaling pathway and burn wound healing ^[1].

Tagln-MerCreMer mouse is generated by replacing part of the coding sequence in exon 2 of the murine Tagln gene with a tamoxifen-inducible MerCreMer recombinase cassette. Before tamoxifen induction, MerCreMer recombinase is confined to the cytoplasm; only after tamoxifen treatment can MerCreMer translocate into the nucleus to exert its genetic recombination function. When Tagln-MerCreMer mice are crossed with mice containing loxP sites, tamoxifen induction triggers Cre-mediated sequence recombination between loxP sites specifically in the smooth muscle of offspring.