Substrates and Inhibitors

A fluorogenic caspase-8/granzyme B substrate containing the benzyloxycarbonyl (Z) moiety.

Caspase 9 is a member of the CED-3 subfamily of the caspase family of cysteine proteases that play an essential role in the execution phase of apoptosis. These enzymes share a dominant primary specificity for cleaving bonds following aspartic acid residues. Initiator caspases (such as caspase 8) activate effector...

Lyophilized powder. Soluble in DMSO. Ac-PAL-AMC is a fluorogenic peptide substrate for measuring caspase-like activity of the immunoproteasome. Hydrolysis of this substrate by the beta1i-subunit of the immunoproteasome is monitored by observing fluorescence at an Excitation wavelength of 345nm and Emission at 445nm....

NFF-3 is a fluorogenic substrate of matrix metalloproteinases (MMPs). NFF-3 is hydrolyzed rapidly by MMP-3 (kcat/Km = 218,000 s-1*M-1) and slowly by MMP-9 (kcat/Km = 10,100 s-1*M-1) with no significant hydrolysis by MMP-1 or MMP-2. NFF-3 can be used to differentiate MMP-3 activity from that of other MMPs.{37000,...

The C2 domain of conventional PKC isoforms mediates calcium-dependent translocation. Peptides from that region can block PKC translocation and inhibit function, both in cells and cell lysates. PKCalpha (C2-4) inhibitor peptide is a synthetic peptide that blocks PKC activity in HepG2 cells stimulated with calcium and...

C188-9 is a STAT3 inhibitor. It binds to the phosphotyrosyl peptide binding site in the STAT3 Src homology 2 (SH2) domain (Ki = 136 nM) and inhibits G-CSF-induced activation of STAT3 in patient-derived acute myeloid leukemia (AML) cells (IC50s = 8-18 µM). C188-9 induces apoptosis in patient-derived AML cells (EC50s...

Ac-QPKK(Ac)-AMC is a fluorogenic substrate for sirtuin 1 (SIRT1), SIRT2, and SIRT3. It is selectively deacylated by SIRT1-3 over SIRT6. Upon enzymatic cleavage by SIRT1, SIRT2, or SIRT3, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify SIRT1, SIRT2, and SIRT3 activity. AMC...

Z-Gly-Pro-AMC is a fluorogenic substrate for the determination of post-proline cleaving enzyme (prolyl endopeptidase).

Ex: 534 nm. Em: 619 nm. Soluble in: DMSO. ProRedT-derived protease substrates are colorless and non-fluorescent. Cleavage of blocking protease-cleavable peptide residue by caspases generates the strongly red fluorescent ProRedT that can be monitored fluorimetrically at ~620 nm with excitation of ~530 nm....

Solid lyophilized powder. Soluble in DMSO. Highly potent and selective cell permeable inhibitor of the proteasome. Inhibits the chymotrypsin-like and caspase-like peptidase activity of the proteasome, Calpain and cathepsin inhibitor, Autophagy activator, Similar structure as MG-132 (AG-CP3-0011) but much higher...

The renin fluorogenic substrate consists of the normal peptide substrate for renin which has been linked to the fluorophore EDANS at one end and to a non-fluorescent quenching molecule (Dabcyl) at the other. After cleavage by renin, the product (peptide-EDANS) is brightly fluorescent and can be easily analyzed using...