Enzyme Substrates

D-Val-Leu-Lys-pNA (D-Val-Leu-Lys-p-nitroanilide) dihydrochloride is a chromogenic peptide substrate that serves as a characteristic substrate for plasmin and plasminogen. D-Val-Leu-Lys-pNA dihydrochloride acts as a sensitive substrate for the DFE27 serine protease derived from Bacillus subtilis DC27. Catalyzed by plasmin, D-Val-Leu-Lys-pNA dihydrochloride binds and hydrolyzes to release p-nitroaniline (pNA), which can be detected colorimetrically at 405 nm as a measure of fibrinolytic activity.

Gly-Arg-AMC is a peptide substrate of DPAP1.

FA-Leu-Gly-Pro-Ala-OH is a furylacryloyl-terminal tetrapeptide that serves as a substrate for bacterial collagenase and spirochete metalloendopeptidase. FA-Leu-Gly-Pro-Ala-OH is specifically hydrolyzed by spirochete collagenase only at the Leu-Gly bond. FA-Leu-Gly-Pro-Ala-OH can be used to determine the equilibrium constant of peptide bond hydrolysis, and also to detect collagenase-mediated cleavage reactions via turbidimetry based on absorbance reduction.

Z-Ala-Arg-Arg-AMC (Fluorogenic Proteasome Substrate) is a fluorogenic substrate for assaying trypsin-like activity of proteasome.

Boc-LRR-AMC (Boc-Leu-Arg-Arg-AMC) is a fluorogenic substrate, which can be utilized for detecting the trypsin-like activity of the 26S proteasome or the 20S proteasome core.

N-Acetyl-Ile-Glu-Pro-Asp-p-nitroanilide (Ac-IEPD-pNA) is a colorimetric peptide substrate of granzyme B that allows accurate measurement of granzyme B activity.

Suc-AAPF-AMC (Suc-Ala-Ala-Pro-Phe-AMC) is a fluorogenic substrate for α-chymotrypsin that can be used for the quantitative determination of chymotrypsin activity (excitation maximum: ~380 nm; emission maximum: ~460 nm).

H-D-Phe-Pip-Arg-pNA hydrochloride (S-2238 hydrochloride) is a specific chromogenic peptide substrate for thrombin (Thrombin). The amide bond of H-D-Phe-Pip-Arg-pNA hydrochloride is rapidly hydrolyzed by thrombin, producing a characteristic yellow absorbance at 405 nm, and the change in absorbance is proportional to thrombin activity. H-D-Phe-Pip-Arg-pNA hydrochloride can be used in biochemical detection-related studies.

MBP MAPK Substrate is used as an exogenous substrate for MAPK.

Bacterial Sortase Substrate III, Abz/DNP TFA is a fluorescent peptide substrate. Bacterial Sortase Substrate III, Abz/DNP TFA undergoes cleavage catalyzed by Staphylococcus aureus sortase A (SrtAΔN24) and Streptococcus pyogenes sortase A (SrtAΔN81), and catalyzes the formation of an amide bond between the carboxyl group of threonine and the amino group of the cell wall cross-bridge. Cleavage of this substrate can be detected at Ex/Em=320 nm/420 nm.

FRETS-VWF73, a 73-amino-acid peptide, is a fluorogenic substrate for ADAMTS13 assay (Ex = 340 nm; Em = 450 nm). FRETS-VWF73 is a predictive tool for thrombotic thrombocytopenic purpura.

Z-Gly-Arg-Thiobenzyl ester is a synthetic peptide substrate used to detect the cleavage activity of C1r. Z-Gly-Arg-Thiobenzyl ester can be cleaved by proteases such as C1r, and when used in combination with DTNB (HY-15915) , it enables colorimetric determination of protease activity, which can be applied to enzymological studies related to the complement system.

Ac-IEPD-AFC is a substrate of Granzyme B.

Pro-Phe-Arg-AMC acetate is a substrate for human glandular kallikrein 2. Pro-Phe-Arg-AMC acetate can be used for the quantitative detection of enzyme activity.

MeOSuc-Arg-Pro-Tyr-pNA (S-2586) is a biological active peptide. (chymotrypsin substrate)

Ac-WLA-AMC is a specific 20S constitutive proteasome β5 fluorogenic substrate.

Hippuryl-His-Leu-OH (N-Benzoyl-Gly-His-Leu) hydrate is a specific substrate for angiotensin-converting enzyme ACE I and is a molecular tool used for ACE activity detection in in vitro experiments. Hippuryl-His-Leu-OH hydrate is hydrolyzed by ACE through competitive binding. Under ACE catalysis, Hippuryl-His-Leu-OH hydrate undergoes hydrolysis to produce hippuric acid (HA). The amount of HA produced can be used to quantitatively assess ACE activity or screen for ACE inhibitors. The His-Leu released from Hippuryl-His-Leu-OH hydrate can also react with o-phthalaldehyde or Fluorescamine (HY-D0715) for fluorescence detection. Hippuryl-His-Leu-OH hydrate can be applied to the in vitro screening of ACE inhibitors for hypertension and cardiovascular diseases, and is also used in the study of changes in ACE activity during physiological and pathological processes such as renal compensatory hypertrophy.

AMARA peptide TFA is a synthetic peptide substrate of sucrose non-fermenting-1-related protein kinase 1 (SnRK1). AMARA peptide TFA contains residues required for SnRK1 phosphorylation, retains the minimal motif recognized by SnRK1, and when this substrate is recognized by cauliflower SnRK1 HRK-A, the hydrophobic residues at the relative positions P-5 and P+4 of the phosphorylated serine require a critical spacing. AMARA peptide TFA can serve as a control substrate in peptide phosphorylation assays for the detection of SnRK1 activity in Arabidopsis thaliana, potato tuber tissues, and during SnRK1 purification.

Ac-DEVD-pNA is a ligand for caspase-3/-7 and related cysteine proteases.

Kemptide is a synthetic heptapeptide that acts as a specific substrate for cAMP-dependent protein kinase (PKA).