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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 (166) and SELPLG Kits (42) and many more products for this protein.
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Mouse (Murine) SELPLG Protein expressed in Human Cells - ABIN2008293
Sako, Chang, Barone, Vachino, White, Shaw, Veldman, Bean, Ahern, Furie: Expression cloning of a functional glycoprotein ligand for P-selectin. in Cell 1994
Show all 5 references for ABIN2008293
Human SELPLG Protein expressed in Human Cells - ABIN2002955
Pouyani, Seed: PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. in Cell 1995
Show all 5 references for ABIN2002955
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 (show SELL Proteins)activated neutrophils via PSGL-1 and L-selectin
In the absence of either PSGL-1 or E- and P-selectin (show SELP Proteins).
P-selectin glycoprotein ligand-1 deficiency augments G-CSF (show CSF3 Proteins) induced myeloid cell mobilization.
In p-selectin (show SELP Proteins) 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 Proteins) completely abrogated leukocyte recruitment.
The PSGL-1-L-selectin (show SELL Proteins) complex-induced signaling effects on neutrophil slow rolling and recruitment in vivo demonstrate the functional importance of this pathway.
P-selectin (show SELP Proteins) ligands are induced on a significant proportion of CD4 (show CD4 Proteins)+ T cells during inflammation within the intestine.
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.
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 Proteins) is reported. It contains a canonical chemokine (show CCL1 Proteins) domain. Chemical shift mapping shows the N-termini of PSGL-1 and CCR7 (show CCR7 Proteins) have overlapping binding sites for CCL19 (show CCL19 Proteins) and binding is competitive.
expression of P-selectin (show SELP Proteins) and P-selectin glycoprotein ligand-1, forming an auto-augmented loop of porcine aortic endothelial cells and platelet activation
Staphylococcal SElX (show SEPX1 Proteins) and SSL6 proteins bind cell surface receptors PSGL-1 and CD47 (show CD47 Proteins), respectively.
SCARB2 (show SCARB2 Proteins) and PSGL-1 in human gastrointestinal tract, lung, and brain tissues correlated with the distribution of pathological changes seen in EV71 infection.
P-selectin glycoprotein ligand-1 and L-selectin (show SELL Proteins) have roles in neutrophil recruitment and activate human endothelial colony-forming cells at the site of vessel injury
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