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Edoxaban impurity 4

  Cat. No.:  DC44168  
Chemical Structure
480452-36-6
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Field of application
Edoxaban impurity 4 is an impurity of Edoxaban. Edoxaban (DU-176) is a selective, potent and orally active factor Xa (FXa) inhibitor with Kis of 0.561 nM and 2.98 nM for free FXa and prothrombinase, respectively. Edoxaban is an anticoagulant agent and can be used for stroke prevention.
Chemicals PropertiesBiological activity COA & MSDSRelated productsDatasheet
Cas No.: 480452-36-6
Chemical Name: Edoxaban impurity 4
SMILES: O=C(OC(C)(C)C)N[C@H]1[C@@H](NC(C(NC2=NC=C(Cl)C=C2)=O)=O)CC[C@H](C(N(C)C)=O)C1
Formula: C21H30ClN5O5
M.Wt: 467.95
Sotrage: 2 years -20°C Powder, 2 weeks 4°C in DMSO, 6 months -80°C in DMSO
MSDS
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MSDS_27850_DC44168_480452-36-6
COA
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Cat. No. Product name Field of application
DC47299 Fitusiran Fitusiran (ALN-AT3SC), an small interfering RNA, specifically targets antithrombin (AT) messenger RNA to lower production of AT in the liver. Fitusiran increases thrombin generation and has the potential for the research of the hemophilia.
DC44168 Edoxaban impurity 4 Edoxaban impurity 4 is an impurity of Edoxaban. Edoxaban (DU-176) is a selective, potent and orally active factor Xa (FXa) inhibitor with Kis of 0.561 nM and 2.98 nM for free FXa and prothrombinase, respectively. Edoxaban is an anticoagulant agent and can be used for stroke prevention.
DC44167 Edoxaban impurity 6 Edoxaban impurity 6 is an impurity of Edoxaban. Edoxaban (DU-176) is a selective, potent and orally active factor Xa (FXa) inhibitor with Kis of 0.561 nM and 2.98 nM for free FXa and prothrombinase, respectively. Edoxaban is an anticoagulant agent and can be used for stroke prevention.
DC28095 O-Desmethyl apixaban sulfate sodium O-Desmethyl apixaban sulfate sodium is a major circulating metabolite of Apixaban in humans. O-Desmethyl apixaban sulfate sodium inhibits factor X (FXa) with a Ki of 58 μM.
DC11231 Zifaxaban Zifaxaban is a novel, potent, selective, direct and oral factor Xa inhibitor with IC50 of 11.1 nM (human FXa), displays > 10,000-fold selectivity than other serine proteases.
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