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SIGLEC1 encodes a member of the immunoglobulin superfamily. Zusätzlich bieten wir Ihnen SIGLEC1 Antikörper (235) und SIGLEC1 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
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the subset of peritoneal CD11b (zeige ITGAM ELISA Kits)(+)CD169(+) macrophages increased and CCL22 (zeige CCL22 ELISA Kits) expression level decreased significantly during the DSS (zeige PMP22 ELISA Kits)-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 (zeige CD8A ELISA Kits)(+) 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 (zeige TGFB1 ELISA Kits)) production.
Viral infection significantly upregulated Siglec1 expression in mouse macrophages in an IFN/JAK (zeige JAK3 ELISA Kits)/STAT1 (zeige STAT1 ELISA Kits) 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.
the antibody-sialidase conjugate desialylated tumor cells in a HER2 (zeige ERBB2 ELISA Kits)-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 (zeige KLRK1 ELISA Kits)).
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 (zeige TRIM21 ELISA Kits) 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.
In colorectal tumor, malignant melanoma, and endometrial tumor, it was shown that a high density of CD169-positive macrophages in the lymph node sinus was a predictive factor for better clinical prognosis.
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 (zeige CD163 ELISA Kits) 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 (zeige CD163 ELISA Kits) 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 (zeige CD163 ELISA Kits) in PRRSV entry.
Clear changes in the quantity of sialoadhesin(+) and CD163 (zeige CD163 ELISA Kits)(+) 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