LAYN Protein, Human, Recombinant (hFc)

Layilin 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 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 the 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. Also, 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. Besides, Layilin might play an important role in the process of invasion and lymphatic metastasis of lung carcinoma.

Pack Size	Availability	Price/USD
100 μg	In stock	$ 451.00
200 μg	5 days	$ 771.00
500 μg	5 days	$ 1,560.00

Biological Information

Testing in progress

Description

Species	Human
Expression System	HEK293
Tag	hFc
Accession Number	Q6UX15-2
Synonyms	layilin
Construction	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.
Protein Purity	> 90 % as determined by SDS-PAGE
Molecular Weight	Approxiamtely 49.5 kDa

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method.
Formulation	Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background	Layilin 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 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 the 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. Also, 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. Besides, Layilin might play an important role in the process of invasion and lymphatic metastasis of lung carcinoma.