All LAYN reagents are produced in house and quality controlled, including 9 LAYN Antibody, 2 LAYN ELISA, 39 LAYN Gene, 7 LAYN Lysate, 7 LAYN Protein, 2 LAYN qPCR. All LAYN reagents are ready to use.
Recombinant LAYN proteins are expressed by HEK293 Cells with fusion tags as C-human IgG1-Fc, C-His, C-cleavage.
LAYNantibodies are validated with different applications, which are ELISA, WB, ELISA(Cap), IHC-P, ELISA(Det).
LAYNcDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each LAYN of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.
LAYNELISA Kit are quality controlled by 8 internation QC standard which guarantee every ELISA Kit with high quality.
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.