Recombinant Human PSGL-1/CD162 Protein (His & Fc Tag) | PKSH031570

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SKU:
575-PKSH031570
€998.00
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Description

Recombinant Human PSGL-1/CD162 Protein (His & Fc Tag) | PKSH031570 | Gentaur US, UK & Europe Disrtribition

Synonyms: P-selectin glycoprotein ligand 1; PSGL-1; Selectin P ligand; CD162; SELPLG;CLA;PSGL1

Active Protein: N/A

Activity: A DNA sequence encoding the extracellular domain (Met1-Val295) of human PSGL-1 precursor (AAC50061.1) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Protein Construction: A DNA sequence encoding the extracellular domain (Met1-Val295) of human PSGL-1 precursor (AAC50061.1) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Fusion Tag: C-His & Fc

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 57.1 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinitycounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~120 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.

Research Area: N/A

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