Mouse PSGL-1 Protein 3029

Additional Information:
inaccessionQ62170|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundP-Selectin glycoprotein ligand-1 (PSGL-1) has long been studied as an adhesion molecule involved in immune cell trafficking and is recognized as a regulator of many facets of immune responses by myeloid cells. PSGL-1 also regulates T cell migration during homeostasis and inflammatory settings.|molecular weightThe protein has a predicted MW of 28.74 kDa. Due to glycosylation, the protein migrates to 68-108 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Mouse PSGL-1 Protein 3029proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceP-Selectin glycoprotein ligand-1 (PSGL-1) has long been studied as an adhesion molecule involved in immune cell trafficking and is recognized as a regulator of many facets of immune responses by myeloid cells. PSGL-1 also regulates T cell migration during homeostasis and inflammatory settings.Protein namesP-Selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162)Gene namesSelplg,Selplg Selp1 SelplMass10090DaFunctionA SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-Selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.Subellular locationCell membrane ; Single-pass membrane protein .TissuesHighly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach.StructureHomodimer; disulfide-linked. Interacts with P- and E-Selectins, through their lectin/EGF domains. Interaction with P-Selectin requires sialyl Lewis X glycan modification and tyrosine sulfation, probably on Tyr-54, for high affinity binding (By similarity). Dimerization appears not to be required for P-Selectin/SELP binding (By similarity). Interacts with SNX20 (By similarity). Interacts with MSN and SYK; mediates SYK activation downstream of SELPLG (By similarity). Interacts with HAVCR1 (By similarity).Post-translational modificationDisplays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1–>4GlcNAcbeta1–>6(Galbeta1–>3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with Selectins and for functioning. No sulfated O-glycans. Some N-glycosylation (By similarity).Target Relevance information above includes information from UniProt accession: Q62170The UniProt Consortium|