Siglec-7/CD328 (C-6His) (recombinant human)

Protein Construction: Recombinant Human Sialic Acid-binding Ig-like Lectin 7 is produced by our Mammalian expression system and the target gene encoding Gln19-Leu353 is expressed with a 6His tag at the C-terminus. Sequence: Gln19-Leu353. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 50-70 kDa. Protein function: Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains. Eleven human Siglecs have been cloned and characterized. Human Siglec-7 encodes a 467 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail. Siglec-7 exists as a monomer on the cell surface and is expressed on natural killer cells, CD8+ T cells and monocytes. It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid. The gene encoding Siglec-7 was mapped to chromosome 19q13.3. Protein function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro). [The UniProt Consortium]