NFF-2

A quenched fluorescence substrate for MMPs. MMP-3 (stromelysin-1) hydrolyzes this substrate (k_cat/K_m = 5.9 x 10⁴ M^-1sec^-1) at a rate 60 times faster than the hydrolysis by MMP-1 (interstitial collagenase). NFF-2 shows little discrimination between MMP-3, MMP-2 (gelatinase-A; k_cat/K_m = 5 x 10⁴ M^-1s^-1), and MMP-9 (gelatinase-B; k_cat/K_m = 5.5 x 10⁴ M^-1s^-1).

A quenched fluorescent substrate for MMPs (excitation maximum: ~325 nm; emission maximum: ~393 nm). MMP-3 (stromelysin-1) hydrolyzes this substrate (k_cat/K_m = 59,400 M^-1s^-1) at a rate 60X faster than hydrolysis by MMP-1 (interstitial collagenase). NFF-2 shows little discrimination between MMP-3, MMP-2 (gelatinase-A; k_cat/K_m = 54,000 M^-1s^-1), and MMP-9 (gelatinase-B; k_cat/K_m = 55,300 M^-1s^-1).

Cell permeable: no

Primary Target
Matrix Metalloproteinases (MMPs)

Product does not compete with ATP.

Reversible: no

kcat/Km = 5.9 x 104 M-1sec-1 as substrates for MMP-3 (stromelysin-1)

Supplied as a trifluoroacetate salt.

Following initial thaw, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

MCA-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(DNP)-NH₂ (DNP = 2,4-dinitrophenyl; Nva = L-norvaline)

Nagase, H., et al. 1994. J. Biol. Chem. 269, 20952.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Toxicity: Standard Handling (A)