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Product
Overview |
Recombinant
Human Layilin, Fc-tagged expressed in human cells is a
disulfide-linked homodimeric protein. The reduced monomer
consists of 437 amino acids and predicts a molecular mass of
49.5 KDa. As a result of glycosylation, the rhLAYN/Fc monomer
migrates as an approximately 60-65KDa protein in SDS-PAGE under
reducing conditions. |
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Description |
Layilin (LAYN),
a recently characterized 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, and its
adjacent LH2-LH3 tandem arrays in the cytoplasmic domain provide
docking sites for talin. 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. 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. A DNA sequence encoding the extracellular domain
(Met 1- Glu 220 ) of human Layilin (NP_849156.1) precursor was
expressed with the C-terminal fused Fc region of human IgG1. |
Abbr.: 
