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SIGLEC1 encodes a member of the immunoglobulin superfamily. Zusätzlich bieten wir Ihnen SIGLEC1 Kits (25) und SIGLEC1 Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 233 products:
Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für FACS, IF - ABIN118291
Kraal, Janse: Marginal metallophilic cells of the mouse spleen identified by a monoclonal antibody. in Immunology 1986
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Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für FACS - ABIN317444
Crocker, Kelm, Dubois, Martin, McWilliam, Shotton, Paulson, Gordon: Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. in The EMBO journal 1991
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Human Monoclonal SIGLEC1 Primary Antibody für FACS, IHC (fro) - ABIN153421
Hartnell, Steel, Turley, Jones, Jackson, Crocker: Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations. in Blood 2001
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Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für FACS, IHC (fro) - ABIN317446
Kaisho, Takeda, Tsujimura, Kawai, Nomura, Terada, Akira: IkappaB kinase alpha is essential for mature B cell development and function. in The Journal of experimental medicine 2001
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Human Monoclonal SIGLEC1 Primary Antibody für FACS - ABIN316948
Kirchberger, Majdic, Steinberger, Blüml, Pfistershammer, Zlabinger, Deszcz, Kuechler, Knapp, Stöckl: Human rhinoviruses inhibit the accessory function of dendritic cells by inducing sialoadhesin and B7-H1 expression. in Journal of immunology (Baltimore, Md. : 1950) 2005
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Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für FACS, WB - ABIN4899472
Honke, Shaabani, Merches, Gassa, Kraft, Ehrhardt, Häussinger, Löhning, Dittmer, Hengel, Recher, Lang, Lang: Immunoactivation induced by chronic viral infection inhibits viral replication and drives immunosuppression through sustained IFN-I responses. in European journal of immunology 2016
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Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für IHC (fro) - ABIN118290
Movita, Kreefft, Biesta, van Oudenaren, Leenen, Janssen, Boonstra: Kupffer cells express a unique combination of phenotypic and functional characteristics compared with splenic and peritoneal macrophages. in Journal of leukocyte biology 2012
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Mouse (Murine) Monoclonal SIGLEC1 Primary Antibody für FACS - ABIN4896153
Lu, Chen, Rong, Yang, Li, Xu, Yu, Wang, Zhang, Shi, Chen: LECT2 drives haematopoietic stem cell expansion and mobilization via regulating the macrophages and osteolineage cells. in Nature communications 2016
CD169(+) macrophages are important contributors to the IFN-I response and thereby influence antiviral activity, CD8 (zeige CD8A Antikörper)(+) 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 Antikörper)) production.
Viral infection significantly upregulated Siglec1 expression in mouse macrophages in an IFN/JAK (zeige JAK3 Antikörper)/STAT1 (zeige STAT1 Antikörper) 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.
Robust infection in lymph nodes and spleen requires CD169, suggesting that a combination of fluid-based movement followed by CD169-dependent trans-infection can contribute to viral spread.
CD169(+) monocytes and macrophages have a critical role in preventing excessive inflammation in renal ischemia-reperfusion injury by downregulating intercellular adhesion molecule-1 (zeige ICAM1 Antikörper) expression on vascular endothelial cells.
results identify CD169(+) macrophages as promoters of high-affinity humoral immune responses and emphasize the value of CD169 as target for Ag delivery to improve vaccine responses
Sialoadhesin is critical for macrophages to phagocytose and clear the sialylated pathogen group B Streptococcus.
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 Antikörper) 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.
Siglec-1 and Siglec-2 (zeige CD22 Antikörper) are potential biomarkers in autoimmune disease. (Review)
Siglec-1 on myeloid cells could fuel novel CD4 (zeige CD4 Antikörper)(+) T-cell infections and contribute to HIV-1 dissemination in vivo.
evidence identifying sialyllactose-containing gangliosides in the viral membrane and the cellular lectin Siglec-1 as critical determinants for HIV-1 capture and storage by mature DCs and for DC-mediated trans-infection of T cells
Our study suggests that HIV-1 capture by CD169 can provide virus evasion from both innate (phagocytosis) and adaptive immune responses
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 Antikörper) 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 Antikörper) 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 Antikörper) in PRRSV entry.
Clear changes in the quantity of sialoadhesin(+) and CD163 (zeige CD163 Antikörper)(+) 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