P-Selectin Protein, Human (HEK293, Fc)

P-selectin, a Ca(2+)-dependent receptor on myeloid cells, crucially binds to sialyl-Lewis X on neutrophils and monocytes, facilitating the interaction of activated endothelial cells or platelets with leukocytes. This engagement, primarily with SELPLG/PSGL1 and PODXL2, is vital for the rapid rolling of leukocytes during early inflammation. P-selectin's interactions with SNX17 further mediate neutrophil adhesion and rolling, dependent on the sialyl-Lewis X epitope and specific tyrosine sulfation on SELPLG. P-Selectin Protein, Human (HEK293, Fc) is the recombinant human-derived P-Selectin protein, expressed by HEK293, with C-hFc labeled tag. The total length of P-Selectin Protein, Human (HEK293, Fc) is 730 a.a., with molecular weight of 130-150 kDa.

P-selectin, a Ca(2+)-dependent receptor on myeloid cells, facilitates the binding to carbohydrates on neutrophils and monocytes, playing a crucial role in the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized by P-selectin is sialyl-Lewis X, and this interaction is pivotal for the rapid rolling of leukocytes over vascular surfaces during the initial stages of inflammation, accomplished through engagement with SELPLG. Additionally, P-selectin forms interactions with SNX17 and mediates adhesion and rolling of neutrophils through its association with SELPLG/PSGL1 and PODXL2. This interaction is contingent on the sialyl-Lewis X epitope of SELPLG and PODXL2, as well as the specific tyrosine sulfation on SELPLG.

Human

HEK293

C-hFc

P16109 (W42-A771)

6403  [NCBI]

130-150 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.