Ac-Gly-BoroPro is a selective FAP inhibitor with a K_i of 23 nM.

Ki: 23 nM (FAP)^[1]

FAP has been implicated in cancer; however, its specific role remains elusive because inhibitors that distinguish FAP from other prolyl peptidases like dipeptidyl peptidase-4 (DPP-4) have not been developed. Ac-Gly-BoroPro selectively inhibits FAP relative to other prolyl peptidases. FAP reacts readily with submicromolar concentrations of Ac-Gly-BoroPro, reaching steady state inhibition levels rapidly (K_i=23±3 nM). In contrast, DPP-4 requires higher Ac-Gly-BoroPro concentrations for inhibition and a longer time to reach steady state inhibition levels (K_i=377±18 nM). Ac-Gly-BoroPro inhibits other prolyl peptidases (DPP-7, DPP-8, DPP-9, prolyl oligopeptidase, and acylpeptide hydrolase) with K_i values ranging from 9- to 5400-fold higher than that for FAP inhibition. The N-acyl-linkage in Ac-Gly-BoroPro blocks the N terminus of the inhibitor, making it less nucleophilic and therefore unlikely to cyclize^[1].

上海金畔生物科技有限公司 has not independently confirmed the accuracy of these methods. They are for reference only.

214.03

C₈H₁₅BN₂O₄

886992-99-0

Ac-Gly-{boroPro}

Ac-G-{boroP}

Room temperature in continental US; may vary elsewhere.

Powder	-80°C	2 years
	-20°C	1 year

*该产品在溶液状态不稳定，建议您现用现配，即刻使用。

In Vitro: 

DMSO : ≥ 50 mg/mL (233.61 mM)

* “≥” means soluble, but saturation unknown.

*

请根据产品在不同溶剂中的溶解度，选择合适的溶剂配制储备液；该产品在溶液状态不稳定，建议您现用现配，即刻使用。

• [1]. Edosada CY, et al. Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity. J Biol Chem. 2006 Mar 17;281(11):7437-44.

K_i values for inhibition of proteases by Ac-Gly-BoroPro are determined using the method of progress curves for analysis of tight binding competitive inhibitors. Various concentrations of Ac-Gly-BoroPro are reacted with FAP (1.0 nM) and DPP-4 (0.1 nM) in the presence of Ala-Pro-AFC (500 μM for FAP; 100 μM for DPP-4), and time-dependent inhibition of each protease is monitored. Reactions contained inhibitor concentrations at least 20-fold greater than protease concentrations, such that the protease-inhibitor complex does not significantly deplete the free inhibitor^[1].

上海金畔生物科技有限公司 has not independently confirmed the accuracy of these methods. They are for reference only.

• [1]. Edosada CY, et al. Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity. J Biol Chem. 2006 Mar 17;281(11):7437-44.