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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 (233) and SELPLG Proteins (13) and many more products for this protein.
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These findings indicate a novel pathway in tumor metastasis, i.e., tumor cell mediated activation of P-selectin (show SELP ELISA Kits) in platelets, followed by activation and secretion of Asm (show SMPD1 ELISA Kits) and in turn release of ceramide and tumor metastasis. The data suggest that p38 MAPK (show MAPK14 ELISA Kits) acts downstream from P-selectin (show SELP ELISA Kits) and is necessary for the secretion of Asm (show SMPD1 ELISA Kits).
Psgl-1 deficiency is protective against the prothrombotic effects of IL-1beta (show IL1B ELISA Kits) .
PSGL-1, CD43, and CD44 moved normally to the uropods of chemokine-stimulated C1galt1(-/-) neutrophils
these results demonstrate that P-selectin (show SELP ELISA Kits) 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 (show SELL ELISA Kits)activated neutrophils via PSGL-1 and L-selectin
In the absence of either PSGL-1 or E- and P-selectin (show SELP ELISA Kits).
P-selectin glycoprotein ligand-1 deficiency augments G-CSF (show CSF3 ELISA Kits) induced myeloid cell mobilization.
In p-selectin (show SELP ELISA Kits) knock-out mice, several antiinflammatory cytokines were significantly increased following peripheral nerve injury.
the presence of endogenous selectin ligands, particularly PSGL-1 on leukocytes, is required for cancer progression.
Data indicate that only the combined deficiency in PSGL-1 and ESL-1 (show GLG1 ELISA Kits) completely abrogated leukocyte recruitment.
The significant presence of CLA+ T cells and E-selectin (show SELE ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) interactions with glycoprotein ligands (CD44 (show CD44 ELISA Kits)/hematopoietic cell E-/L-selectin (show SELL ELISA Kits) ligand and PSGL-1) mediate the initial capturing of cells out of flow.
CD162 staining and the staining degree, with the other standard immunohistochemical stains, were shown to be beneficial in the diagnosis of multiple myeloma disease.
The solution structure of CCL19 (show CCL19 ELISA Kits) is reported. It contains a canonical chemokine (show CCL1 ELISA Kits) domain. Chemical shift mapping shows the N-termini of PSGL-1 and CCR7 (show CCR7 ELISA Kits) have overlapping binding sites for CCL19 (show CCL19 ELISA Kits) and binding is competitive.
expression of P-selectin (show SELP ELISA Kits) and P-selectin glycoprotein ligand-1, forming an auto-augmented loop of porcine aortic endothelial cells and platelet activation
Staphylococcal SElX (show SEPX1 ELISA Kits) and SSL6 proteins bind cell surface receptors PSGL-1 and CD47 (show CD47 ELISA Kits), respectively.
SCARB2 (show SCARB2 ELISA Kits) and PSGL-1 in human gastrointestinal tract, lung, and brain tissues correlated with the distribution of pathological changes seen in EV71 infection.
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.
selectin P ligand
, P-selectin glycoprotein ligand 1
, P-selectin glycoprotein ligand 1 propeptide
, cutaneous lymphocyte-associated associated antigen
, leukocyte cell surface adhesion molecule
, selectin, platelet (p-selectin) ligand
, P-selectin glycoprotein ligand-1
, synaptotagmin-like protein 1