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SIGLEC1 encodes a member of the immunoglobulin superfamily. Additionally we are shipping SIGLEC1 Antibodies (220) and SIGLEC1 Kits (22) and many more products for this protein.
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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.
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 (show ICAM1 Proteins) 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.
prion (show PRNP Proteins) pathogenesis was unaltered in sialoadhesin-deficient mice
CD169(-/-) mice demonstrated an enhanced response to antigen-pulsed exosomes. This is the first report of a role for CD169 in the capture of exosomes and its potential to mediate the immune response to exosomal antigen.
Siglec-1 can interact with SR-BI (show SCARB1 Proteins) in the phagocytosis of oxLDL by macrophages, rather than act as an independent receptor for oxLDL.
Siglec-1 on myeloid cells could fuel novel CD4 (show CD4 Proteins)(+) 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
GM3 (show GRM6 Proteins)-CD169 binding is a gp120 (show ITIH4 Proteins)-independent signal for sequestration and preservation of HIV-1 infectivity.
The most abundant cytokine present in semen (TGF-beta1 (show TGFB1 Proteins)) is able to enhance specifically the expression of an important molecule (CD169) involved in the capture and transmission of HIV-1 particles from the mucosal lumen to the submucosal compartment.
Siglec-1 may play a proinflammatory role in stimulating lymphocyte proliferation and activation in rheumatoid arthritis.
CD169(+) macrophages in RLNs promote CD8 (show CD8A Proteins)(+) T-cell-mediated antitumor immunity.
downregulation of CD169 expression or neutralizing CD169 function abrogated dendritic cell-mediated HIV-1 capture and trans infection, while exogenous expression of CD169 in receptor-naive cells rescued glycosphingolipid-dependent capture and trans infection.
Based on increased SIGLEC1 expression in circulating monocytes, findings suggest a role for SIGLEC1 in the chronic progressive phases of multiple sclerosis.
the CD169/Sn endocytic pathway is conserved and capable of presenting lipid antigens to iNKT cells
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