Human LAYN ELISA Kit sinobiological KIT10208

$714.00
In stock
SKU
KIT10208
Catalog No.SizePrice (USD)
KIT10208-11 Kit (96 Tests)$740.55

General Information

Product nameHuman LAYN ELISA Kit
SpecificityRecognizes both recombinant and natural Human Layilin / LAYN
ConjugateHRP
ShippingThis ELISA Kit is shipped at ambient temperature.
StorageUnopened Kit: Store at 2 - 8℃ Opened/Reconstituted Reagents: Please refer to CoA
Assay typeSolid Phase Sandwich ELISA (quantitative)
Sample typeLysate
Sensitivity2.29 pg/mL
Assay range15.63-1000 pg/mL
Materials provided1. 96 well microplate coated with Capture Antibody 2. Detection Antibody conjugated to HRP 3. Standards 4. Wash Buffer Concentrate 5. Dilution Buffer Concentrate 6. Color Reagent A 7. Color Reagent B 8. Stop Solution
Product overviewThis Human LAYN ELISA Kit is an enzyme-linked immunosorbent assay for the quantitative measurement of Human LAYN protein in Lysate . It contains recombinant Human LAYN, and antibodies raised against the recombinant protein. This ELISA kit is complete and ready-to-use.

Synonyms: FLJ30977 ELISA Kit, Human; FLJ31092 ELISA Kit, Human; UNQ208/PRO234 ELISA Kit, Human

Image / Experimental Information

Image 1 DescriptionThis standard curve is only for demonstration purposes. A standard curve should be generated for each assay.
Image 1 Alt TextHuman Layilin / LAYN ELISA Kit Standard Curve 50
Image 1 URLSource image

Background Information

Full Namelayilin
DescriptionLayilin 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.
References
  1. 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.
  2. Bono P, et al. (2001) Layilin, a novel integral membrane protein, is a hyaluronan receptor. Mol Biol Cell. 12(4)891-900.
  3. Bono P, et al. (2005) Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin. Exp Cell Res. 308(1):177-87.
  4. Scoles DR. (2007) The merlin interacting proteins reveal multiple targets for NF2 therapy. Biochim Biophys Acta. 1785(1):32-54.
  5. 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.
  6. 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.

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