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SELPLG encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. Additionally we are shipping SELPLG Antibodies (263) and SELPLG Kits (32) and many more products for this protein.
Showing 9 out of 13 products:
Studies indicate that P-selectin glycoprotein ligand-1 (PSGL-1) PSGL-1 can negatively regulate T cell function.
Results suggest that PSGL-1 may play an oncogenic role in the development of intestinal tumors, and this is likely mediated through activation of NFkB signaling by MIP (show TNPO1 Proteins)-1g.
c-Myc (show MYC Proteins) regulates P-selectin glycoprotein ligand-1 expression in monocytes during HIV-1 infection.
The percentage of CXCR3 (show CXCR3 Proteins)(+) CD4 (show CD4 Proteins)(+) TEM (show CYLD Proteins) cells negatively correlated with the severity of the cutaneous disease in psoriasis patients. Importantly CLA(+) CD4 (show CD4 Proteins)(+) TCM cells expressing CCR6 (show CCR6 Proteins)(+) or CCR4 (show CCR4 Proteins)(+)CXCR3 (show CXCR3 Proteins)(+) negatively correlated with psoriasis severity suggesting recruitment to the skin compartment.
Platelet-leukocyte aggregations increased in acute ischemic stroke patients rapidly within 3h. The I allele of PSGL-1 M62I was associated with risk of developing acute ischemic stroke, especially large artery atherosclerosis stroke and small artery occlusion stroke. Small artery occlusion stroke patients with the II genotype of PSGL-1 M62I have the higher level of platelet-neutrophil aggregates.
The significant presence of CLA+ T cells and E-selectin (show SELE Proteins) expressions in the OLPG suggests their involvement in the etiopathogenesis of OLP; however, only a weak correlation between CLA+ T cells and E-selectin (show SELE Proteins) was observed.
PSGL-1 is a novel receptor for S. pneumoniae that contributes to protection against invasive pneumococcal disease.
This study provides a better understanding of the biology of P-selectin (show SELP Proteins) and PSGL-1 and their roles in dissemination and resensitization of Multiple myeloma treatment.
Report influence of SELPLG variation on leukocyte-platelet interactions in cardiovascular disease.
E-selectin (show SELE Proteins) interactions with glycoprotein ligands (CD44 (show CD44 Proteins)/hematopoietic cell E-/L-selectin (show SELL Proteins) ligand and PSGL-1) mediate the initial capturing of cells out of flow.
results indicate that P-selectin (show SELP Proteins) deletion significantly decreases tumor stiffness in Rip1 (show RALBP1 Proteins)-Tag2 mice by inhibiting LOX (show LOX Proteins) expression.
this study shows that PSGL-1 plays a fundamental role in balancing viral control and immunopathology and also functions to regulate T cell responses in the tumor microenvironment
Psgl-1 deficiency accelerates bleomycin-induced lung fibrosis and inflammation in mice through activating the PI3K/AKT (show AKT1 Proteins) axis.
Circulating soluble P-selectin (show SELP Proteins) must dimerize to promote inflammation and thrombosis in mice.
The results from the present study suggest that activated platelets secrete Pselectin to promote cardiac inflammation and fibrosis in Ang (show ANG Proteins) IIinduced hypertension.
These findings indicate a novel pathway in tumor metastasis, i.e., tumor cell mediated activation of P-selectin (show SELP Proteins) in platelets, followed by activation and secretion of Asm (show SMPD1 Proteins) and in turn release of ceramide and tumor metastasis. The data suggest that p38 MAPK (show MAPK14 Proteins) acts downstream from P-selectin (show SELP Proteins) and is necessary for the secretion of Asm (show SMPD1 Proteins).
Psgl-1 deficiency is protective against the prothrombotic effects of IL-1beta (show IL1B Proteins) .
PSGL-1, CD43, and CD44 moved normally to the uropods of chemokine-stimulated C1galt1(-/-) neutrophils
these results demonstrate that P-selectin (show SELP Proteins) expression on ECs is regulated in part by glycosylation mechanisms and that glycosylation inhibitors efficiently reduce the adhesion of sRBCs and leukocytes to ECs.
endothelial colony-forming cells interact with activated neutrophils via PSGL-1 and L-selectin (show SELL Proteins)
This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
P-selectin glycoprotein ligand 1
, cutaneous lymphocyte-associated associated antigen
, selectin P ligand
, P-selectin glycoprotein ligand 1 propeptide
, P-selectin glycoprotein ligand-1
, leukocyte cell surface adhesion molecule
, selectin, platelet (p-selectin) ligand