P2Y1 Protein, Human (Sf9, FLAG)

The P2Y1 protein acts as a receptor for extracellular adenine nucleotides, specifically ADP. In platelets, ADP binding activates phospholipase C, leading to intracellular calcium mobilization, platelet shape changes, and aggregation. P2Y1 Protein, Human (Sf9, FLAG) is the recombinant human-derived P2Y1 protein, expressed by Sf9 insect cells , with N-Flag labeled tag. The total length of P2Y1 Protein, Human (Sf9, FLAG) is 372 a.a., .

The P2Y1 receptor serves as a receptor for extracellular adenine nucleotides, particularly ADP. Upon binding to ADP, this receptor, found notably in platelets, triggers the mobilization of intracellular calcium ions through the activation of phospholipase C. Consequently, this activation induces changes in platelet shape and, ultimately, platelet aggregation. ATP acts as an antagonist, inhibiting the ADP-induced mobilization of calcium ions. Specific antagonists of the P2Y1 receptor, such as A3P5PS, A3P5P, and A2P5P, have been identified and shown to impede downstream signaling events mediated by the mobilization of calcium ions from intracellular stores, as well as platelet shape changes in response to extracellular ADP.

Human

Sf9 insect cells

N-Flag

P47900 (T2-L373)

5028

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.