LAYN recombinant protein

LAYN Protein, Rhesus, Recombinant (hFc Tag)

Cat. Num. AAA8123563

• Purity: >90% as determined by SDS-PAGE
• Synonyms: LAYN; LAYN Protein; Rhesus; Recombinant (hFc Tag); Rhesus Layilin/LAYN Protein (Fc Tag); layilin; LAYN recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >90% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Glu220

• Species: Rhesus
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Ala 22
• Tag: C-human IgG1-Fc
• Protein Construction: A DNA sequence encoding the rhesus LAYN (XP_001105766.1)(Met1-Glu220) was expressed with the Fc region of human IgG1 at the C-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; 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.

SDS-Page

Related Product Information for LAYN recombinant protein

Background: Layilin recently characterized as a 55kDa 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.

References

Borowsky ML, et al. (1998) Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles.J Cell Biol. 143(2):429-42.Bono P, et al. (2001) Layilin, a novel integral membrane protein, is a hyaluronan receptor. Mol Biol Cell. 12(4)891-900.Bono P, et al. (2005) Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin. Exp Cell Res. 308(1):177-87.Scoles DR. (2007) The merlin interacting proteins reveal multiple targets for NF2 therapy. Biochim Biophys Acta. 1785(1):32-54.Chen Z, et al. (2008) Down-regulation of layilin, a novel hyaluronan receptor, via RNA interference, inhibits invasion and lymphatic metastasis of human lung A549 cells. Biotechnol Appl Biochem. 50(Pt 2):89-96.Wegener KL, et al. (2008) Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain. J Mol Biol. 382(1):112-26.

NCBI and Uniprot Product Information

• Molecular Weight: The recombinant Rhesus LAYN is a disulfide-linked homodimer. The reduced monomer comprises 440 amino acids and has a calculated molecular mass of 49.8kDa.The apparent molecular mass of the protein is approximately 58kDa respectively in SDS-PAGE.
• Protein Family: Layilin