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Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Additionally we are shipping and many more products for this protein.
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indicate that Siglec-9 (show SIGLEC9 Antibodies) affects several different signaling pathways in IL-4 (show IL4 Antibodies)-stimulated macrophages, which resulted in enhanced induction of Arg1 (show ARG1 Antibodies) in Siglec-9 (show SIGLEC9 Antibodies)-expressing RAW264 cells
Competitive ELISA assays confirmed the involvement of sulfated (show SULF1 Antibodies) epitopes in the affinity between Siglec-E and cruzipain, probably modified by natural protein environment
Data indicate a role for neuraminidase 1 (Neu1 (show NEU1 Antibodies)) in regulating Siglec E protein-toll-like receptor 4 (TLR4 (show TLR4 Antibodies)) interaction and endotoxemia.
Siglec-E-deficient macrophages showed a propensity toward a tumor-promoting M2 polarization, indicating a secondary role of CD33 (show CD33 Antibodies)-related Siglecs in limiting cancer-promoting inflammation and tumor growth.
siglec-E functions as an inhibitory receptor of neutrophils via positive regulation of NADPH oxidase (show NOX1 Antibodies) activation and ROS (show ROS1 Antibodies) production
These results suggest that sSiglec-9 has an antitumor benefit against MUC1 (show MUC1 Antibodies)-expressing tumor in the transgenic mice.
Siglec-9 (show SIGLEC9 Antibodies) expressed on immune cells may play a role as a potential counterreceptor for MUC1 (show MUC1 Antibodies) and that this signaling may be another MUC1 (show MUC1 Antibodies)-mediated pathway and function in parallel with a growth factor-dependent pathway.
Siglec-E is induced in a MyD88 (show MYD88 Antibodies)-dependent manner. Once up-regulated, it can control TLR-dependent NF-kappaB (show NFKB1 Antibodies) antiviral responses by directly inhibiting TLR-induced antiviral cytokine production.
Putative adhesion molecule that mediates sialic-acid dependent binding to cells. 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.
, SIGLEC-like 1
, myeloid inhibitory siglec
, sialic acid binding Ig-like lectin 5
, sialic acid-binding Ig-like lectin 12
, sialic acid-binding Ig-like lectin 5
, sialic acid-binding Ig-like lectin E
, sialic acid-binding Ig-like lectin-like 1
, sialic acid-binding immunoglobulin-like lectin E