156143-97-4

Upstream product

• 156143-96-3 [4-(3-Acetylsulfanyl-2-tert-butoxycarbonylamino-propyl)-cyclohexyl]-acetic acid ethyl ester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 7398-81-4 (4-bromomethylphenyl)acetic acid ethyl ester 
• 156143-93-0 2-Amino-3-(4-ethoxycarbonylmethyl-cyclohexyl)-propionic acid ethyl ester 
• 156143-77-0 2-Amino-3-(4-ethoxycarbonylmethyl-phenyl)-propionic acid ethyl ester 
• 156143-95-2 [4-(2-tert-Butoxycarbonylamino-3-hydroxy-propyl)-cyclohexyl]-acetic acid ethyl ester 
• 156143-94-1 2-tert-Butoxycarbonylamino-3-(4-ethoxycarbonylmethyl-cyclohexyl)-propionic acid ethyl ester 
• 156143-76-9 2-(Benzhydrylidene-amino)-3-(4-ethoxycarbonylmethyl-phenyl)-propionic acid ethyl ester 

Downstream Products

• 156143-99-6 (R,S)-1,1'-dithiobis<2-amino-3-<4-(carboxymethyl)cyclohexyl>propane>, bis(trifluoroacetate) 

Relevant academic research and scientific papers

Investigation of the active site of aminopeptidase A using a series of new thiol-containing inhibitors

Aminopeptidase A (APA) and aminopeptidase N (APN) are two metallopeptidases which have been suggested to be involved in the enzymatic cascade of the renin-angiotensin system. APA liberates angotensin III from angiotensin II by releasing the N-terminal asp