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SIGLEC1 encodes a member of the immunoglobulin superfamily. Additionally we are shipping SIGLEC1 Antibodies (260) and SIGLEC1 Kits (35) and many more products for this protein.
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the subset of peritoneal CD11b (show ITGAM Proteins)(+)CD169(+) macrophages increased and CCL22 (show CCL22 Proteins) expression level decreased significantly during the DSS (show PMP22 Proteins)-induced colitis
A new subset of resident macrophages in the intestinal muscularis externa was discovered, identified as iba1(pos) CD169(neg).
the capacity of CD169(+) macrophages to contain the parasite burden and its sequestration into different tissues and to limit infection-induced inflammation is crucial to mitigating Plasmodium infection and pathogenesis
apoptosis contributes to both tolerance and immunity, as well as establishing CD169 as a critical mediator of the immune response to extracellular vesicles.
CD169(+) macrophages are important contributors to the IFN-I response and thereby influence antiviral activity, CD8 (show CD8A Proteins)(+) T-cell exhaustion and immunopathology.
Although CD169 participates in the immune response to tumour antigen and appears to be a positive prognostic marker for human cancers, its role in modulating melanoma growth and metastasis is less clear.
Inhibition of Siglec-1 can prevent atherosclerotic lesion formation by suppress monocytes-endothelial cells adhesion and macrophages accumulation.
Data show that knockdown of sialic acid binding Ig-like lectin 1 (siglec-1) in RAW 264.7 macrophage resulted in inhibiting the production of transforming growth factor beta 1 (TGF-beta1 (show TGFB1 Proteins)) production.
Viral infection significantly upregulated Siglec1 expression in mouse macrophages in an IFN/JAK (show JAK3 Proteins)/STAT1 (show STAT1 Proteins) pathway-dependent manner.
Siglec-1 is a key receptor for macrophage/lymphocyte trans-infection of surface-bound virions, and the N-acyl side chain of sialic acid is a critical determinant for the Siglec-1/MLV interaction.
Our findings evidenced for the first time the novel association between SIGLEC1 rs3859664 SNP and active pulmonary TB. Intriguingly, carriers of the polymorphism produced less IL-1ss than non-carriers, suggesting the possible involvement of Siglec-1 signalling pathway with inflammasome complex.
the antibody-sialidase conjugate desialylated tumor cells in a HER2 (show ERBB2 Proteins)-dependent manner, reduced binding by natural killer (NK) cell inhibitory sialic acid-binding Ig-like lectin (Siglec) receptors, and enhanced binding to the NK-activating receptor natural killer group 2D (NKG2D (show KLRK1 Proteins)).
The results reveal marked differences between afferent and efferent ymphatic endothelial cells and identify molecules on lymphatic vessels. Further characterizations of Siglec-1 (CD169) and macrophage scavenger receptor 1 (MSR1/CD204), show that they are discriminatively expressed on lymphatic endothelium of the subcapsular sinus but not on lymphatic vasculature of the lymphatic sinus
High CD169 expression is associated with HIV-1.
CD169 expression in regional LNs was not associated with PSA-relapse.
These results highlight the importance of sialic acids on the V1V2 region in binding to sialic acid-binding immunoglobulin-like lectin.
High expression of SIGLEC1 in pregnant women with autoantibodies against Ro/SS-A (show TRIM21 Proteins) indicates an enhanced risk for autoimmune congenital heart block development.
These data demonstrate a prominent role for Siglec-1 in the internalization of HIV-1 to the virus-containing compartment in infected monocyte-derived macrophages
These findings suggest that CD169+ macrophages in RLNs might be a useful marker for assessing clinical stage, including LN states, in patients with breast cancer.
CD169 might act as a co-stimulatory molecule for cytotoxic T-cell activation, and could define a population of tumour-infiltrating macrophages with potential anti-tumour properties in human hepatocellular carcinoma tissues.
the transcription initiation site for sialoadhesin (Siglec-1), which is a porcine alveolar macrophage-specific gene, was determined by 5' rapid amplification of cDNA end.
Fusion protein of sialoadhesin and domains 5-9 of CD163 (show CD163 Proteins) receptors blocked the respiratory syndrome virus infection.
European genotype porcine reproductive and respiratory syndrome virus inhibits porcine alveolar macrophages phagocytosis in vitro, through the interaction with its internalization receptor sialoadhesin.
After infection, PRRSV viremia in SIGLEC1(-/-) pigs followed the same course as in SIGLEC1(-/+) and SIGLEC1(+/+) littermates. The absence of SIGLEC1 had no effect on other aspects of PRRSV infection, including disease course and histopathology.
Endodomain-deletion mutants of sialoadhesin promoted porcine reproductive and respiratory syndrome virus infection less efficiently.
). These results provided fundamental evidence for CD163 (show CD163 Proteins) and SN as two functional candidate genes affecting immunity in pigs.
effect of antibody binding to pSn on macrophage viability, phagocytosis of microspheres, uptake and processing of soluble antigens, reactive oxygen/nitrogen species production, MHC I and MHC II cell surface expression and cytokine production
Porcine sialoadhesin (CD169/Siglec-1) is an endocytic receptor that allows targeted delivery of toxins and antigens to macrophages.
Sialoadhesin is confirmed as a PRRSV (porcine reproductive and respiratory syndrome virus)internalization receptor and is shown to interact with CD163 (show CD163 Proteins) in PRRSV entry.
Clear changes in the quantity of sialoadhesin(+) and CD163 (show CD163 Proteins)(+) macrophages in the placentas and organs of embryos/fetuses during gestation.
This gene encodes a member of the immunoglobulin superfamily. The encoded protein is a lectin-like adhesion molecule that binds glycoconjugate ligands on cell surfaces in a sialic acid-dependent manner. It is a type I transmembrane protein expressed only by a subpopulation of macrophages and is involved in mediating cell-cell interactions. Alternative splicing produces a transcript variant encoding an isoform that is soluble rather than membrane-bound\; however, the full-length nature of this variant has not been determined.
, sheep erythrocyte receptor
, sialic acid-binding Ig-like lectin 1
, sialic acid-binding immunoglobulin-like lectin 1
, Sialic acid-binding Ig-like lectin 1