Layilin Isoform 2 Extracellular Domain (human, recombinant)

Layilin is a C-type lectin receptor. It is composed of an extracellular region that contains the C-type lectin homology domain, a transmembrane domain, and a cytoplasmic domain. Layilin is ubiquitously expressed and localizes to the cell surface, but has also been found in mitochondria. It is involved in cell migration, the epithelial-to-mesenchymal transition (EMT), and antitumor immunity and binds to the extracellular matrix proteins hyaluronan and glycosylated collagen, as well as the cytoskeleton-membrane linker proteins talin, merlin, and radixin. The layilin isoform 2 extracellular domain binds to melanoma cells in a calcium-dependent manner. Knockout of LAYN prevents the accumulation of lymph node-derived CD8+ tumor-infiltrating lymphocytes (TILs) in a competitive adoptive transfer murine colon adenocarcinoma model. Layilin protein levels are increased in CD8+ TILs that highly express programmed cell death protein 1 (PD-1) and cytotoxic T lymphocyte protein 4 (CTLA-4) isolated from patients with metastatic melanoma. Cayman's Layilin Isoform 2 Extracellular Domain (human, recombinant) protein consists of 437 amino acids, has a calculated molecular weight of 49.5 kDa, and a predicted N-terminus of Ala22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 60-65 kDa due to glycosylation.Synonyms: LAYN. Purity: >90% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Recombinant C-terminal human IgG1 Fc-tagged layilin isoform 2 extracellular domain expressed in HEK293 cells. Amino Acids: 22-220. MW: 49.5 kDa. Formulation: (Request formulation change), Lyophilized from sterile 50 mM Tris, pH 7.5, with 100 mM glycine and 10 mM sodium chloride. UniProt Accession #: Q6UX15.