Siglec-7 Protein, Human (HEK293, His)

Siglec-7 protein, identified as a putative adhesion molecule, serves as a mediator of sialic-acid dependent cellular binding. It exhibits a preference for binding to alpha-2,3- and alpha-2,6-linked sialic acid, along with interactions with disialogangliosides such as disialogalactosyl globoside, disialyl lactotetraosylceramide, and disialyl GalNAc lactotetraoslylceramide. Notably, the sialic acid recognition site of Siglec-7 may undergo masking due to cis interactions with sialic acids on the same cell surface. In immune responses, it functions as an inhibitory receptor, inducing tyrosine phosphorylation upon ligand binding and recruiting cytoplasmic phosphatases through their SH2 domains, thereby blocking signal transduction and inhibiting natural killer cell cytotoxicity. Siglec-7 may also play a role in hemopoiesis, inhibiting the differentiation of CD34+ cell precursors towards the myelomonocytic cell lineage and impeding the proliferation of leukemic myeloid cells in vitro. Additionally, it interacts with PTPN6/SHP-1 upon phosphorylation.