|Human cell-derived rhLayilin extracellular domain (Catalog#10208-H08H)|
|0.2 μm filtered solution in PBS|
|This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human Layilin (rhLayilin; Catalog#10208-H08H; aa 1-220; NP_849156.1). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.|
This antibody can be used at 1:1000-1:2000 with the appropriate secondary reagents to detect Human layilin.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Anti-Histone H3 rabbit monoclonal antibody at 1:200 dilution
Lane A: NIH3T3 Whole Cell Lysate
Lane B: Hela Whole Cell Lysate
Lysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution.
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size:15 kDa
Observed band size:17 kDa
Layilin, a recently characterized as a 55 kDa transmembrane protein with homology to C-type lectins, is present in numerous cell lines and tissue extracts. As one of the adaptor proteins, talin mediates the interactions between the actin filaments and the cell membrane by binding to integral membrane proteins and to the cytoskeleton. Layilin is a newly identified membrane-binding site for talin in peripheral ruffles of spreading cells, a ten-amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding, and its adjacent LH2-LH3 tandem arrays in the cytoplasmic domain provide docking sites for talin. Furthermore, talin binds layilin, PIPK1gamma and integrins in similar although subtly different ways. Layilin binds specifically to hyaluronan (HA) through its extracellular domain, a ubiquitous extracellular matrix component in most animal tissues and body fluids, but not to other tested glycosaminoglycans. The research suggests that layilin may mediate signals from extracellular matrix to the cell cytoskeleton via interaction with different intracellular binding partners and thereby be involved in the modulation of cortical structures in the cell. All the above actions reveal an interesting parallel between layilin and the known HA receptor CD44. In addition, merlin and radixin have been identified as different intracellular binding partners of layilin. Accordingly, it has been suggested that layilin plays roles in a variety of cellular processes, including cell shape, adhesion, motility, and homeostasis, as well as signal transduction. In addition, layilin might play an important role in the process of invasion and lymphatic metastasis of lung carcinoma.