Name :
Recombinant Human PSGL-1/CD162 Protein (His & hFc Tag)
Biological Activity :
Background :
P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinity ounter-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 ~12 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.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
AAC50061.1
NCBI Gene ID :
Synonyms :
Synonyms :
selectin P ligand
Amino Acid Sequence :
Molecular Weight :
The recombinant human PSGL-1/Fc is a disulfide-linked homodimer after removal of the signal peptide and the prppeptide. The reduced monomer consists of 526 amino acids and has a predicted molecular mass of 57.1 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh PSGL-1/Fc monomer is approximately 110-120 kDa due to glycosylation.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
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.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
CD162 Protein, Human; CLA Protein, Human; PSGL-1 Protein, Human; PSGL1 Protein, Human PSGL-1/CD162 背景信息 P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinity ounter-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 ~12 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.
References & Citations :
1. Sako, D. et al., 1993, Cell. 75: 1179-1186. 2. Wilkins, P. P. et al., 1995, J. Biol. Chem. 270: 22677-22680. 3. Frenette, P. S. et al., 2000, J. Exp. Med. 191: 1413-1422. 4. Vandendries, E.R .et al., 2004, Thromb. Haemost. 92: 459-466.. 5. Pouyani, T. et al., 1995, Cell. 83: 333-343.
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