PSGL-1 / CD162 / SELPLG Protein

16.05.2013

Sino Biological Inc. liefert PSGL-1 / CD162 / SELPLG Protein mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über PSGL-1 / CD162 / SELPLG Protein lesen Sie bitte: http://www.sinobiological.com/PSGL-1-CD162-SELPLG-Protein-g-11720.html

Produkt-Information von PSGL-1 / CD162 / SELPLG Protein

Synonym	SELPLG
Protein Construction	A DNA sequence encoding the human SELPLG (Q14242) (Met1-Gly295) with a C-terminal polyhistidine tag was expressed.
Source	Human
Expression Host	Human Cells

QC Testing von PSGL-1 / CD162 / SELPLG Protein

Purity	(82+15.2)% as determined by SDS-PAGE	SDS-PAGE: SELPLG protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Leu 18
Molecular Mass	The recombinant human SELPLG comprises 289 amino acids and has a predicted molecular mass of 30.5 kDa. The apparent molecular mass of the protein is approximately 89 and 61 kDa in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. Please contact us for any concerns or special requirements.

Usage Guide von PSGL-1 / CD162 / SELPLG Protein

Storage	Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Beschreibung von PSGL-1 / CD162 / SELPLG Protein

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.

References

Sako D. et al., 1993, Cell. 75: 1179-86.
Wilkins P P. et al., 1995, J Biol Chem. 270: 22677-80.
Frenette P S. et al., 2000, J Exp Med. 191: 1413-22.
Vandendries ER .et al., 2004, Thromb Haemost. 92: 459-66.
Pouyani T. et al., 1995, Cell. 83: 333-43.