3D-VAA-54849 - suc-dedededededededeahxdpeg2dpeg2drdrdrdrdrdrdrdrdrahxdkcy5-nh2

Substrate for chymotrypsin, also used for the identification of this enzyme by enzymoblotting.

Suc-AAA-pNA, a readily soluble and sensitive substrate for human and rat neutrophil and porcine pancreatic elastases. The trialanine substrate is also hydrolyzed by proteinase K, subtilisins and thermitase as well as by astacin, a crayfish zinc-endopeptidase.

Suc-GGF-pNA was used to determine the activity of chymotrypsin and of Streptomyces griseus protease B.

A readily soluble, specific and sensitive substrate for chymotrypsin and human pancreatic elastase. It is also hydrolyzed by cathepsin G and chymase. Furthermore it is the standard substrate for FK-506 binding proteins (FKBPs, also called macrophilins) and cyclophilins, which belong to the group of peptidyl prolyl cis-trans isomerases (PPIases). Thus, Suc-AAPF-pNA has been used for an uncoupled protease-free assay of PPIase activity.

Suc-AAV-pNA (SAAVNA), a very specific substrate for human and rat neutrophil elastases.

Suc-AAPL-pNA, a sensitive substrate for human and especially porcine pancreatic elastases. Substrate for leucine endopeptidase from the psychrotropic bacillus B. cereus.

Suc-GPLGP-AMC, a highly sensitive, fluorogenic substrate for thimet oligopeptidase (collagenase-like peptidase, Pz-peptidase, metalloendopeptidase 24.15) as well as for post-proline cleaving enzyme (prolyl endopeptidase).

A highly sensitive fluorogenic substrate for plasmin. Suc-AFK-AMC was also used for assaying gingipain K.

The highly sensitive, fluorogenic substrate Suc-GP-AMC is suitable for the determination of prolyl endopeptidase (postproline cleaving enzyme) activity.

Suc-APA-AMC, a sensitive substrate for human neutrophil elastase.

Suc-AAA-AMC, sensitive fluorogenic substrate for pancreatic elastase.

Suc-AAF-AMC, a highly sensitive fluorogenic chymotrypsin substrate. It is also hydrolyzed by neutral metalloendopeptidases, such as thermolysin and enkephalinase (neprilysin, NEP 24.11). Suc-AAF-MCA has also been used for the chymotrypsin-like activity of the 20S proteasome.

Suc-AAVA-pNA has been used for assaying hamster chymase 2.

Suc-FLF-thiobenzyl ester, a very sensitive substrate for the determination of cathepsin G activity. It is also cleaved by chymotrypsin, chymotrypsin-like serine proteases from skin as well as rat mast cell proteases.

Suc-AAPM-pNA, a sensitive substrate for human pancreatic elastase.

Substrate for porcine calpain isozymes I and II and for E.coli protease Ti. Suc-LY-AMC is cleaved by a hyperthermostable subtilisin-type protease bound to the surface layer of the archaeon Staphylothermus marinus.

A very sensitive substrate for rat mast cell proteases and chymotrypsin. Suc-AAPF-SBzl is also cleaved by human leukocyte cathepsin G and chymotrypsin-like serine proteases from skin.

The fluorogenic substrate Suc-LLVY-AMC is used for measuring the chymotrypsin-like activity of the 20S proteasome, in combination with e.g. Bz-VGR-AMC (for assaying its trypsin-like activity) and Z-LLE-AMC (for determining its PGPH activity). Suc-LLVY-AMC is also cleaved by a chymotrypsin-like enzyme from sperm extract of the ascidian Halocynthia roretzi, a strong inhibitor of fertilization. The substrate has also been used to analyze the chymotrypsin-like activity of trypsins as well as chymase from rat mast cells. Furthermore, Suc-LLVY-AMC is a substrate for carboxypeptidase Y, proteinase yscE (kexin), ingensin, as well as for porcine calpain isozymes I and II and for papain.

The peptidylprolyl isomerase substrate Suc-AAPF-AMC is also hydrolyzed by carboxypeptidase Y, cathepsin G, and chymotrypsin. Suc-AAPF-AMC has also been used to analyze the chymotrypsin-like activity of trypsins.

This enzyme substrate was used to test the concept of substrate-assisted catalysis with an engineered bacterial serine endopeptidase, subtilisin. Suc-FAAF-pNA has been employed for assaying subtilisins from psychrophilic bacteria and myroilysin, a metalloproteinase from the deep sea bacterium Myroides profundi.