factor xa

RabbitFactor Xa is produced from purified Rabbit Factor X through activation by Russells' Viper Venom, followed by the removal of the venom.

CanineFactor Xa is derived from purified Canine Factor X through activation by Russell's Viper Venom, after which the venom is removed.

RatFactor Xa is derived from the activation of purified Rat Factor X using Russells' Viper Venom. Following activation, Russells' Viper Venom is removed.

D-Pro-Phe-Arg-Chloromethylketone, an inhibitor of coagulation factor XII and plasma kallikrein, is significant in the regulation of thrombosis and inflammation [1].

Boc-Ile-Glu-Gly-Arg-AMC (IEGR-AMC) is a specific, highly fluorogenic substrate for clotting enzyme factor Xa (coagulation factor Xa) and is also hydrolyzed by acrosin from the ascidian Halocynthia roretzi.

Ciraparantag acetate, an anticoagulant reversal agent, is a small molecule specifically designed to bind noncovalently by charge-charge interaction to unfractionated heparin and low-molecular-weight heparin. It shows binding characteristics that are similar to those of direct oral anticoagulants (DOACs).

Delparantag( PMX-60056) is a heparins antidote designed to restore coagulation.

Methoxycarbonyl-D-Nle-Gly-Arg-pNA is a synthetic trypsin substrate used for coagulation factors IXa (FIXa) and Xa (FXa), as demonstrated by studies [1] [2] [3].

cMCoFx1 is an effective and selective FXIIa cyclic peptide inhibitor. It exhibits high binding affinity for FXIIa (KD: 900 pM) and potent inhibitory activity (Ki: 370 pM). cMCoFx1 effectively suppresses the intrinsic coagulation pathway, demonstrates high stability in serum, and shows no cytotoxicity.

Suc-Ile-Glu(γ-pip)-Gly-Arg-pNA hydrochloride is a chromogenic substrate specifically designed for factor Xa.

NFF-3 TFA, a selective matrix metalloproteinase (MMP) substrate, specifically interacts with MMP-3 and MMP-10 for hydrolysis. Additionally, it undergoes cleavage by trypsin, hepatocyte growth factor activator, and factor Xa. When labeled with the CyDye pair, Cy3/Cy5Q, NFF-3 TFA generates fluorescence in cell assays, facilitating the detection of cell activity [1].

Boc-Leu-Gly-Arg-AMC is a specific fluorogenic substrate designed for the enzymatic detection and quantification of complement component C3/C5 convertases, coagulation factor Xa, and soybean trypsin-like enzyme activity. Boc-Leu-Gly-Arg-AMC is also susceptible to hydrolysis by macropain, a high molecular weight thiol proteinase isolated from human erythrocytes, making it a versatile tool for enzymatic assays.

Thrombin is a "trypsin-like" serine protease that is encoded by the F2 gene in humans. Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). Thrombin in turn acts as a serine protease that converts soluble