SIGLECL1

GWB-78AAA1

Peptide with sequence C-EAIGYEYSEINIPK from the C Terminus of the Notes: Peptide ELISA: antibody detection limit dilution 1:128 000. Western Blot: Preliminary experiments gave no signal but low background in Human PBMC and Molt-4 lysates at up to 1ug/ml. Summary: Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This protein is a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein upon tyrosine phosphorylation has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This protein is located in a cluster with other SIGLEC3-like genes on 19q13. 4. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene. [1] Angata T. Varki N. M. and Varki A. et al. A second uniquely human mutation affecting sialic acid biology[2] Yu Z. Lai C. M. Maoui M. Banville D. and Shen S. H. et al. Identification and characterization of S2V a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs[3] Foussias G. Taylor S. M. Yousef G. M. Tropak M. B. Ordon M. H. and Diamandis E. P. Cloning and molecular characterization of two splice variants of a new putative member of the Siglec-3-like subgroup of Siglecs