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SIGLEC5 encodes a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. Additionally we are shipping SIGLEC5 Antibodies (167) and SIGLEC5 Kits (7) and many more products for this protein.
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An unbiased screen revealed Hsp70 (show HSP70 Proteins) as a ligand for Siglec-5 and Siglec-14 (show SIGLEC14 Proteins). Hsp70 (show HSP70 Proteins) stimulation through Siglec-5 delivers an anti-inflammatory signal, while stimulation through Siglec-14 (show SIGLEC14 Proteins) is pro-inflammatory.
Data indicate that the Siglec-5/14 genotype influences neutrophil responses to group B Streptococcus.
we found that secretory IgA is taken up by M cells via the Dectin-1 (show CLEC7A Proteins) receptor, with the possible involvement of Siglec-5 acting as a co-receptor.
These studies demonstrate the Siglec5 carbohydrate recognition domain alone is sufficient for binding sialylated carbohydrates and provide a foundation for further investigation of Siglec5 structure and function.
Siglec-5 expression protects T cells from HIV-1- and apoptosis-induced cell death and contributes to the different outcomes of HIV-1 infection in humans and chimpanzees.
Human Siglec-5 inhibitory receptor and immunoglobulin A (IgA) have separate binding sites in streptococcal beta protein.
Siglec-5 expression correlates with lack of proliferation in a subset of human cells, and is upregulated by activation of chimpanzee but not human lymphocytes.
expression of Siglec-5 on cells of the myelomonocytic lineage and alteration of its expression by inflammatory stimuli suggest a role for this protein in cell/cell interactions following microbial exposure.
Siglec-5 can be classified as an inhibitory receptor with the potential to mediate SHP-1 and/or SHP-2-dependent signaling in the absence of tyrosine phosphorylation.
Siglecs-5 did not interact with sulfate derivatives of LacNAc and sulfated (show SULF1 Proteins) oligosaccharides containing sialic acid.
The Siglec-E-deficient dendritic cells were defective for TRIF (show RNF138 Proteins)-mediated IFN-beta (show IFNB1 Proteins) production in response to E. coli infection.
This study demonstrated that virulent parasite Leishmania donovani (AG83+Sias) establish a unique sialic acids-mediated binding and subsequent phagocytosis in the host cell through the selective exploitation of siglec-1 (show SIGLEC1 Proteins).
Immunohistochemical analysis of the Peyer's patches (PPs (show INPP5K Proteins)) tissue sections shows that Siglec-F is expressed on the surface of the Intestinal microfold (M) cell membrane exposed to the intestinal lumen.
new data relating to the structure and function of Siglec-E, the major CD33 (show CD33 Proteins)-related Siglec expressed on mouse neutrophils, monocytes, macrophages, and dendritic cells.
indicate that Siglec-9 (show SIGLEC9 Proteins) affects several different signaling pathways in IL-4 (show IL4 Proteins)-stimulated macrophages, which resulted in enhanced induction of Arg1 (show ARG1 Proteins) in Siglec-9 (show SIGLEC9 Proteins)-expressing RAW264 cells
Competitive ELISA assays confirmed the involvement of sulfated (show SULF1 Proteins) epitopes in the affinity between Siglec-E and cruzipain, probably modified by natural protein environment
These data identify a previously unrecognized endogenous anti-inflammatory property of airway mucins by which their glycans can control lung eosinophilia through engagement of Siglec-F.
Data indicate a role for neuraminidase 1 (Neu1 (show NEU1 Proteins)) in regulating Siglec E protein-toll-like receptor 4 (TLR4 (show TLR4 Proteins)) interaction and endotoxemia.
Siglec-E-deficient macrophages showed a propensity toward a tumor-promoting M2 polarization, indicating a secondary role of CD33 (show CD33 Proteins)-related Siglecs in limiting cancer-promoting inflammation and tumor growth.
depending on the nature of the allergy model used, the negative regulatory role of siglec-F on eosinophilia may be overridden.
This gene encodes a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. These cell surface lectins are characterized by structural motifs in the immunoglobulin (Ig)-like domains and sialic acid recognition sites in the first Ig V set domain. The encoded protein is a member of the CD33-related subset of Siglecs and inhibits the activation of several cell types including monocytes, macrophages and neutrophils. Binding of group B Streptococcus (GBS) to the encoded protein plays a role in GBS immune evasion.
sialic acid binding Ig-like lectin 5
, CD33 antigen-like 2
, OB-binding protein 2
, obesity-binding protein 2
, sialic acid-binding Ig-like lectin 5
, sialic acid-binding immunoglobulin-like lectin 5
, sialic acid binding Ig-like lectin F
, sialic acid-binding Ig-like lectin F
, sialic acid-binding lectin Siglec-F
, SIGLEC-like 1
, myeloid inhibitory siglec
, sialic acid-binding Ig-like lectin 12
, sialic acid-binding Ig-like lectin E
, sialic acid-binding Ig-like lectin-like 1
, sialic acid-binding immunoglobulin-like lectin E