• glycan
  • Rescreening on a more expanded glycan array reconfirmed this finding, but also identified a second closely related ligand in which the fucose is absent (NeuAcα2-3(6-O-sulfo)Galβ1-4GlcNAc, or 6′-sulfated sialyl N-acetyl-D-lactosamine. (wikipedia.org)
  • Each lectin domain is specific for the linkage that connects sialic acid to the glycan. (wikipedia.org)
  • neutrophils
  • Neutrophils and eosinophils bind to E-selectin. (wikipedia.org)
  • Eosinophils, like neutrophils, use sialylated, protease-resistant structures to bind to E-selectin, although the eosinophil expresses much lower levels of these structures on its surface. (wikipedia.org)
  • CD33
  • Amino acids 42-159 of human CD33 were used as the immunogen for the antibody. (novusbio.com)
  • CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. (novusbio.com)
  • The drug is a recombinant, humanized anti-CD33 monoclonal antibody (IgG4 κ antibody hP67.6) covalently attached to the cytotoxic antitumor antibiotic calicheamicin (N-acetyl-γ-calicheamicin) via a bifunctional linker (4-(4-acetylphenoxy)butanoic acid). (wikipedia.org)
  • homology
  • Analysis of this homology has revealed that the lectin domain, which binds sugars, is most conserved, suggesting that the three selectins bind similar sugar structures. (wikipedia.org)
  • carbohydrate
  • As the leukocyte rolls along the blood vessel wall, the distal lectin-like domain of the selectin binds to certain carbohydrate groups presented on proteins (such as PSGL-1) on the leukocyte, which slows the cell and allows it to leave the blood vessel and enter the site of infection. (wikipedia.org)
  • cells
  • CCR7 upregulation allows DCs to migrate to local LNs where they encounter T cells ( 3 ), and depending on their activation state, they can induce a variety of immunogenic or tolerogenic responses ( 4 , 5 ). (jimmunol.org)
  • different
  • Though they share common elements, their tissue distribution and binding kinetics are quite different, reflecting their divergent roles in various pathophysiological processes. (wikipedia.org)