ARG70892

Human CD162 / PSGL1 recombinant protein (hFc-tagged and His-tagged, C-ter)

Human CD162 / PSGL1 recombinant protein (hFc-tagged and His-tagged, C-ter) for SDS-PAGE

Overview

Product Description HEK293 expressed, Human hFc-tagged and His-tagged (C-ter) CD162 / PSGL1 recombinant protein
Tested Application SDS-PAGE
Target Name CD162 / PSGL1
Species Human
A.A. Sequence Thr81 - Glu170
Expression System HEK293
Alternate Names SELPLG; Selectin P ligand; PSGL1; P-selectin glycoprotein ligand 1; PSGL-1; CD162; CLA; CD antigen CD162

Properties

Form Powder
Buffer PBS
Reconstitution It is recommended to reconstitute the lyophilized protein in sterile water to a concentration approximately 1 mg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely.
Storage Instruction For long term, lyophilized protein should be stored at -20°C or -80°C, protected from light and moisture, for up to 12 months. After reconstitution , aliquot and store at 2 to 8°C for up to 2 days, or at -20°C or -80°C for up to 3 months Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening.

Bioinformation

Gene Symbol SELPLG
Gene Full Name Selectin P ligand
Background CD162 (P-selectin glycoprotein ligand-1, PSGL-1) is a sialomucin constitutively expressed as a disulfide-linked homodimer of two 120 kDa subunits on the surface of circulating leukocytes. CD162 serves as a ligand for P- E- and L-selectin, with the highest affinity for P-selectin. It is thus involved in leukocyte rolling at the endothelial surfaces, prerequisite for firm leukocyte adhesion and subsequent transendothelial migration. CD162 also mediates leukocyte-platelet adhesion and interleukocyte contacts. Whereas serving as an adhession molecule on mature leukocytes, CD162 is a potent negative regulator of human hematopoietic progenitors.
Function A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. [UniProt]. [UniProt]
Cellular Localization Cell membrane. [UniProt]
PTM Displays 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 in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation. Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling. [UniProt]