Ac-LETD-AFC is a caspase-8 fluorogenic substrate. Ac-LETD-AFC can measure caspase-8 fluorogenic activity and can be used for the research of cancer cell apoptosis and oxidative stress metabolism.

Ac-ATAD-AFC(Caspase-12 Substrate) is a fluorogenic substrate for caspase-12.

S-2222 (Bz-Ile-Glu-Gly-Arg-pNA HCl) is a chromogenic substrate specifically designed for the detection and measurement of Factor Xa activity.

Gly-Pro-pNA is a chromogenic substrate specifically cleaved by dipeptidyl peptidase IV (DPP IV), an enzyme present in circulation. The enzymatic activity can be measured colorimetrically by detecting the release of p-nitroanilide at 405 nm. DPP IV plays a critical role in inactivating two key peptides, glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide 1 (GLP-1), which are essential for nutrient-stimulated insulin secretion. This substrate is particularly useful for screening DPP IV inhibitors, which are being explored as potential antidiabetic therapeutics.

Cephalofurimazine (CFz) is a NanoLuc substrate optimized for enhanced brain performance. When paired with Antares luciferase, it generates over 20 times more signal from the brain compared to the traditional combination of D-luciferin and firefly luciferase.

Fluorofurimazine is an advanced furimazine derivative with enhanced aqueous solubility, allowing for greater signal output compared to furimazine in bioluminescence imaging. This compound supports higher substrate concentrations and delivers improved sensitivity for in vivo optical imaging applications.

Hydrofurimazine is a NanoLuc substrate whose enhanced aqueous solubility allows delivery of higher doses to mice. Hydrofurimazine enables sensitive bioluminescence imaging for either prolonged light production of high sensitivity.

ViviRen is a synthetic analog of coelenterazine specifically designed for bioluminescence imaging (BLI), offering enhanced performance in visualizing biological processes.

pyCTZ (Pyridyl CTZ) TFA, a pyridyl-modified derivative of Coelenterazine (CTZ), serves as an ATP-independent substrate for LumiLuc luciferase. This compound produces intense blue bioluminescence upon interaction with luciferases and is particularly effective in aequorin-based calcium sensing applications.

Furimazine, an imidazopyrazinone-based substrate, generates exceptionally bright luminescence when paired with NanoLuc (Nluc). This combination produces a 2.5 million-fold increase in light output compared to the Oluc-19 and Coelenterazine system in mammalian cells.

Coelenterazine is a luminescent enzyme substrate, used for monitoring reporter genes in BRET, ELISA and HTS techniques.

Coelenterazine E serves as a bioluminescent probe, widely utilized for its ability to emit light in biological and chemical applications.

Coelenterazine h, a modified form of Coelenterazine, exhibits heightened sensitivity to Ca2+ compared to the native compound, making it an effective tool for detecting subtle fluctuations in Ca2+ concentrations.

pyCTZ (Pyridyl CTZ) hydrochloride, a pyridyl derivative of Coelenterazine (CTZ), functions as an ATP-independent substrate for LumiLuc luciferase. This compound produces intense blue bioluminescence when interacting with luciferases and is particularly useful in aequorin-based calcium sensing applications.

Coelenteramine 400a (Bisdeoxycoelenterazine), a structural analog of Coelenterazine, serves as a substrate for Renilla luciferase (RLuc). When interacting with Coelenteramine 400a, RLuc catalyzes the emission of blue light with a peak wavelength of 395 nm.

H-D-Phe-Pip-Arg-pNA (S-2238) hydrochloride, a chromogenic substrate, is patterned after the N-terminal portion of the A alpha chain of fibrinogen, which is the natural substrate of thrombin. H-D-Phe-Pip-Arg-pNA hydrochloride is specific for thrombin and is used to measure antithrombin-heparin cofactor (AT-III). The AT-III assay using H-D-Phe-Pip-Arg-pNA hydrochloride is sensitive, accurate, and easy to perform.

Z-D-Arg-Gly-Arg-pNA is a colorimetric substrate for Factor Xa.Factor Xa preferentially binds to and cleaves the Arg-Gly-Arg (RGR) peptide sequence to release p-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of Factor Xa activity.

For-Met-Leu-pNA is an N-formylated peptide substrate specifically designed for use in deformylase activity assays, providing a reliable tool for studying enzyme function.

Ac-Phe-Gly-pNA is a synthetic peptide substrate specifically tailored for detecting chymotrypsin activity, offering high specificity for this enzyme.

Z-Gly-Pro-pNA is a synthetic peptide substrate specifically designed for assessing the inhibitory activity of prolyl endopeptidase (PEP), making it a useful tool in enzymatic studies.

RETF-4NA TFA, a highly sensitive and selective substrate for chymase, effectively measures chymase activity both in its free form and when complexed with α2-macroglobulin (α2M). Its specificity makes it a valuable tool for studying chymase-related biochemical processes.

The synthetic peptide Suc-Gly-Gly-Phe-pNA serves as a specific substrate for the enzyme chymotrypsin, demonstrating a Michaelis constant (Km) of 1.6 mM. This value reflects the substrate concentration at which the enzyme achieves half of its maximum reaction rate, indicating its affinity for the peptide.

D-Val-Gly-Arg-p-nitroaniline (D-VGR-pNA)​ is a synthetic chromogenic peptide substrate specifically designed for assessing the enzymatic activity of tissue plasminogen activator (tPA), including its isoforms tPA I and tPA II. Upon cleavage by tPA, the release of p-nitroaniline (pNA) generates a measurable colorimetric signal, enabling precise quantification of amidolytic activity. This substrate is widely utilized in biochemical assays to study tPA’s role in fibrinolysis and to evaluate its enzymatic kinetics in both research and diagnostic applications.

Ac-WEAD-pNA is a colorimetric substrate for caspase-1 and caspase-4.

Ac-DEVD-pNA is a colorimetric substrate for caspase-3 (CPP32) and related cysteine proteases.

Ac-IETD-pNA is a substrate for caspase-8.Caspase-8 preferentially binds to and cleaves the Ile-Glu-Thr-Asp (IETD) peptide sequence to release p-nitroalinide, which can be quantified by colorimetric detection at 405 nm as a measure of enzyme activity.