Mouse Layilin Ectodomain Antibody

Layilin (named after the L-A-Y-I-L-I amino acid motif in the transmembrane segment) is a member of the animal C-type lectin family (1). The mouse Layilin cDNA encodes a 402 amino acid (aa) type I transmembrane protein that, based on the orthologous molecule in hamster, contains a 19 aa signal sequence, a 211 aa extracellular domain (ECD), a 30 aa transmembrane segment, and a 141 aa cytoplasmic tail (2, 3). The ECD of mouse Layilin shares 85%, 70%, and 77% aa sequence identity with that of hamster, rat, and human Layilin, respectively. The ECD includes one carbohydrate recognition domain that contains a single potential Ca⁺⁺-binding site (3). The intracellular region contains three types of LH (Layilin Homology) repeats: three 16‑18 aa LH1 repeats, three 5 aa LH2 repeats, and one 4 aa LH3 repeat (3). Adjacent LH2-LH3 tandem arrays provide docking sites for the actin cytoskeleton adaptor proteins talin, merlin, and radixin (3, 4, 5). Layilin interacts with the ubiquitous extracellular matrix component hyaluronan but not with heparin, chondroitin sulfate, or N-acetyl glucosamine (6). Layilin is widely expressed and localizes to ruffling edges in spreading and migrating cells (3, 5). It does not localize to focal contacts and does not interact with the focal contact proteins alpha -actinin, vinculin, tensin, paxillin, tubulin, or Integrin beta 1 (3).