Background:

(Z-Ala-Ala-Ala-Ala)2Rh110 is a fluorogenic elastase substrate.

Elastase can break down elastin that is an elastic fibre that, together with collagen and can determine the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A of E. coli and other Gram-negative bacteria. In addition, elastase has the critical immunological role of breaking down Shigella virulence factors.

In vitro: (Z-Ala-Ala-Ala-Ala)2Rh110 has been identified as a very sensitive fluorogenic elastase substrate. The colorless and nonfluorescent Z-Ala-Ala-Ala-Ala)2Rh110 was found to be selectively cleaved by elastase to yield the highly fluorescent compound rhodamine 110, which exhibited excellent spectral properties matching the optimal detection window of most fluorescence instruments. After cleavage, Abs(max) is at 497 nm and Em(max) is at 520 nm for rhodamine 110 [1].

In vivo: Currently, there is no animal in vivo data reported.

Clinical trial: So far, no clinical study has been conducted.

Reference:
[1] A.  F. Johnson, M. D. Struthers, K. B. Pierson, et al. Nonisotopic DNA detection system employing elastase and a fluorogenic rhodamine substrate. Analytical Chemistry 65, 2352-2359 (1993).