Pyr-Arg-Thr-Lys-Arg-AMC 

Pyr-Arg-Thr-Lys-Arg-AMC is a AMC peptide, and a fluorescent substrate. Pyr-Arg-Thr-Lys-Arg-AMC can be used to detect the activity of specific proteases, such as Furin, Trypsin, and Thrombin^[1][2][3][4].

Pyr-Arg-Thr-Lys-Arg-AMC s hydrolyzed by purified recombinant PC2 from PC2 and 21 kDa 7B2-transfected CHO cells^[1].
Pyr-Arg-Thr-Lys-Arg-AMC (100 μM; overnight) is cleaved by purified recombinant PC2 with a K_m of 131 μM, indicating a similar enzymatic reaction mechanism to other PC2 peptide substrates^[2].
Pyr-Arg-Thr-Lys-Arg-AMC (10 μM; 4 h) serves as a functional fluorogenic substrate for furin-like proteases across multiple mammalian cell lines, including fruit bat and human cells^[3].
Pyr-Arg-Thr-Lys-Arg-AMC (0.1-400 μM; 15 min-24 h) is cleaved by purified recombinant mouse PC5 from baculovirus-infected Sf9 cells^[4].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

827.93

C₃₇H₅₇N₁₃O₉

155575-02-3

{Pyr}-Arg-Thr-Lys-{Arg-AMC}

{Pyr}-RTK-{Arg-AMC}

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Lamango NS, et al. Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2. Arch Biochem Biophys. 1996 Jun 15;330(2):238-50.

  [2]. Wang W, et al. Cleavage of CCK 33 by recombinant PC2 in vitro. Biochem Biophys Res Commun. 1997 Feb 3;231(1):149-52.

  [3]. El Najjar F, et al. Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host. PLoS One. 2015;10(2):e0115736. Published 2015 Feb 23.  [Content Brief]

  [4]. Cain BM, et al. Production, purification, and characterization of recombinant prohormone convertase 5 from baculovirus-infected insect cells. Protein Expr Purif. 2002;24(2):227-233.  [Content Brief]