Lyso-sulfatide (bovine)

Lyso-sulfatide (0-50 μM; 3 min) inhibits fXa-induced coagulation in normal human plasma with an IC₅₀ of ~26 μM, without affecting thrombin-mediated clot formation^[1].
Lyso-sulfatide (bovine) inhibits prothrombin activation by the human fXa/fVa/PC/PS prothrombinase complex with an IC₅₀ of approximately 0.6 μM, without affecting the amidolytic activity of fXa or thrombin (IIa)^[1].
Lyso-sulfatide (bovine) inhibits prothrombin activation mediated by human fXa/PC/PS in the absence of fVa with an IC₅₀ of 35 μM, showing markedly reduced potency relative to its inhibitory activity in the presence of fVa; it also suppresses prothrombin activation by human gd‑fXa/fVa/PC/PS with an IC₅₀ of 12 μM^[1].
Lyso-sulfatide (bovine) (37-185 μM (flowed over BEGR-fXaᵢ); 18-92 μM (flowed over BEGR-gd-fXaᵢ)) binds specifically to immobilized inactivated human fXa (K_d = 83 μM) and immobilized inactivated human gd-fXa (K_d = 36 μM), with no binding observed to inactive fVIIa, fIXa, or via N-acetyl sulfatide^[1].
Lyso-sulfatide (bovine) binds dansylated inactive human fXa and triggers reversible fluorescence reduction with EC₅₀ values of 50 μM (with PC/PS vesicles) and 80 μM (without PC/PS vesicles); it also suppresses fVa‑induced fluorescence changes of fXa pre‑bound to PC/PS vesicles, indicating inhibition of fVa binding or fVa‑mediated fXa conformational change^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.