Search by product name, CAS, target or catalog number. Press Down Arrow to reach product suggestions, Tab to move between links, and Escape to close suggestions.
USD – US Dollar✓Current currency
Account
Enzyme Activity Probes & Substrates
Browse substrates and optical reporter reagents for enzyme-activity assays. Enzyme-activated fluorogenic probes can convert a chemical transformation into a fluorescence readout.[1] Choose the exact reagent for your enzyme, sample and detection method, and distinguish fluorescent from color-based readouts. This collection does not imply that every substrate is selective for one enzyme or suitable for use in living cells.
CrBKA is a fluorogenic small-molecule substrate specifically designed for SIRT6, a member of the sirtuin family of NAD+-dependent deacetylases. This compound exhibits weak activity, making it suitable for probing SIRT6 enzymatic function in various biological contexts. Its application in research includes the study of cellular metabolism, aging, and the modulation of gene expression through deacetylation processes.
Ac-QPKK(Ac)-AMC is a fluorogenic substrate specifically designed for sirtuin enzymes, facilitating the study of sirtuin-mediated deacetylation processes. This reagent enables the quantitative analysis of sirtuin activity, making it a valuable tool for investigating the role of sirtuins in various biological processes and disease states, including aging and metabolic disorders. Researchers can leverage Ac-QPKK(Ac)-AMC to explore sirtuin function in high-throughput screening assays and in-depth mechanistic studies.
Myosin Light Chain Kinase Substrate (smooth muscle) is a synthetic peptide designed to specifically target and serve as a substrate for smooth muscle myosin light chain kinase (MLCK). This substrate facilitates the study of MLCK activity and its role in smooth muscle contraction mechanisms. It is essential for assays related to muscle physiology, cellular signaling pathways, and the development of therapeutic strategies targeting smooth muscle disorders.
ARI-3144 is a specific substrate for fibroblast activation protein (FAP), designed for effective detection and quantification. When coupled with the fluorophore 7-Amino-4-methylcoumarin (AMC), this substrate facilitates sensitive analysis of FAP activity in various biological samples. ARI-3144 is valuable in research applications related to cancer biology and tissue remodeling, enabling deeper insights into FAP functions and its role in disease progression.
Ac-Phe-Thiaphe-OH is a modified peptide designed as a substrate for carboxypeptidase A (CPA). This compound serves as a valuable tool in enzymatic assays, allowing for the study of CPA activity and substrate specificity. Its incorporation of thiaphenyl enhances interactions, providing insights into peptide cleavage mechanisms and enzyme kinetics. Suitable for biochemical research applications focused on proteolytic enzymes.
Suc-AAP-Abu-pNA is a specific substrate for pancreatic elastase, displaying a Km of 100 μM and a Kcat/Km of 35,300 s-1 M-1 for rat pancreatic elastase, and a Km of 30 μM with a Kcat/Km of 351,000 s-1 M-1 for porcine pancreatic elastase. This colorimetric substrate enables precise measurement of elastase activity in various biological samples. In addition to its enzymatic applications, Suc-AAP-Abu-pNA has been shown to promote oligodendrocyte precursor cell (OPC) migration, making it valuable in research focused on neurobiology and tissue repair.
Ala-Ala-Phe-AMC is a fluorogenic substrate primarily used for the detection of proteolytic activity. Its positively charged characteristics enhance its suitability for various biochemical assays, enabling researchers to investigate protease function in biological samples. This compound is valuable in studies related to protein turnover, cellular signaling, and disease mechanisms involving proteolysis.
Gly-Asp-Asp-Asp-Asp-Lys-β-naphthylamide (GD4K-na) serves as a substrate for human enteropeptidase, exhibiting a Km value of 0.16 mM. This peptide substrate is utilized in studies of protein digestion and enzymatic activity, crucial for understanding the role of enteropeptidase in digestive processes. Its specificity makes GD4K-na valuable in biochemical assays and research applications focused on proteolytic enzymes.
4-Methylumbelliferyl β-D-Glucopyranoside serves as a fluorogenic substrate specifically for β-glucosidase, facilitating the measurement of β-glucosidase activity in various biological assays. Upon enzymatic cleavage, it releases 4-methylumbelliferone, a highly fluorescent compound with an emission maximum between 445-454 nm. The excitation wavelength of 4-methylumbelliferone is influenced by pH, showing peaks at 330, 370, and 385 nm at pH 4.6, 7.4, and 10.4, respectively, making it a valuable tool for studying enzyme kinetics and related research applications.
MMP-1 Substrate is a selective substrate for matrix metalloproteinase-1 (MMP-1) designed for the fluorometric detection of MMP-1 enzymatic activity. This reagent facilitates the assessment of MMP-1 function in various biological samples, enabling studies related to tissue remodeling, inflammation, and cancer research. The substrate's specificity makes it a valuable tool for investigating MMP-1 activity in diverse experimental settings.
MMP-2/MMP-9 Substrate is a synthetic chromogenic polypeptide designed to mimic the cleavage sites of matrix metalloproteinases 2 and 9, also known as gelatinases A and B, within collagen. Upon hydrolysis by collagenase, this substrate interacts with 4,4'-dithiodipyridine or Ellman's Reagent through its thiol group, resulting in a detectable product with distinct ultraviolet absorption characteristics. It is a valuable tool for studying MMP activity and has applications in research related to tissue remodeling, cancer metastasis, and inflammatory processes.
TNO211 is a fluorogenic substrate designed for the specific detection of matrix metalloproteinase (MMP) activity. It contains a cleavable Gly-Leu bond, allowing for the precise identification of MMPs, and features a fluorophore/quencher pair consisting of EDANS and Dabcyl. This reagent operates optimally at excitation/emission wavelengths of 340/485 nm, making it suitable for various applications in biochemical and molecular biology research focused on MMP functions.
MMP-13 Substrate serves as a specific substrate for matrix metalloproteinase-13 (MMP-13), facilitating the study of this enzyme's role in various biological processes. Its primary application lies in the investigation of osteoarthritis (OA), allowing researchers to explore MMP-13 activity in cartilage degradation and remodeling. This substrate is essential for understanding the molecular mechanisms underlying OA progression and potential therapeutic targets.
Dnp-PLGLWAr-NH2 is a synthetic substrate designed specifically for collagenase and gelatinase activity. This reagent can be utilized to quantify total matrix metalloproteinase (MMP) activity in samples treated with APMA. Its effective targeting of collagenolytic enzymes makes it a valuable tool for research into extracellular matrix remodeling and related biological processes.
TNO003 is a selective fluorogenic substrate that specifically targets stromelysin-1 (MMP-3). This reagent exhibits superior selectivity for MMP-3 over other matrix metalloproteinases, including MMP-1, MMP-2, MMP-7, MMP-8, MMP-9, and MMP-13. TNO003 is suitable for quantitative determination of stromelysin activity and can be utilized in fluorescence-based assays at an excitation/emission wavelength of 360/490 nm.
Z-Ala-Arg-Arg-AMC is a fluorogenic proteasome substrate designed to specifically assay the trypsin-like activity of the proteasome. Its unique structure allows for sensitive detection of proteolytic activity, making it a valuable tool for studying protein degradation and turnover in cellular processes. This substrate is widely utilized in research applications focused on proteasome function and its implications in various diseases.
Z-Leu-Leu-Leu-AMC is a fluorogenic substrate designed for the assessment of chymotrypsin-like protease activity in the 20S proteasome. It provides a sensitive and specific means to monitor proteasomal function and proteolytic activity. This reagent is valuable for research applications involving protein degradation, cellular homeostasis, and the study of proteasome-related diseases.
Calpain substrate is a fluorogenic substrate specifically designed for the assessment of calpain enzymatic activity. It is membrane non-permeable, ensuring precise measurement of calpain activity in biological samples. This reagent is suitable for applications in cellular signaling research and studies investigating calpain's role in various physiological and pathological processes.
Ac-KQKLR-AMC TFA is a substrate peptide for Cathepsin S, conjugated with the fluorescent indicator AMC (Excitation/Emission = 354 nm/442 nm). This reagent facilitates the measurement of Cathepsin S activity, enabling researchers to study proteolytic processes and assess enzyme function in various biological contexts. Its application is crucial for investigations into the role of Cathepsin S in physiological and pathological conditions.
Ac-KQL-AMC is a fluorogenic substrate designed to quantify Trypsin-like activity. Upon cleavage by the proteasome, it produces a detectable fluorescence, making it a valuable tool for studying proteolytic activities in various biological contexts. This compound is particularly useful in research applications focused on protein degradation and turnover mechanisms.
Boc-Ala-Gly-Pro-Arg-AMC is a fluorogenic substrate designed for monitoring protease activity, particularly within serine proteases. This substrate is ideal for assessing enzymatic function in research applications involving protease activity, such as studying the oligopeptide enzyme B of Trypanosoma brucei. Its fluorescence allows for sensitive detection of enzymatic events, making it a valuable tool in biochemical and molecular biology studies.
NQEQVSP is a peptide derived from fibrin-binding proteins that acts as a substrate for Factor XIIIa. This compound is specifically recognized by Factor XIII and is enzymatically conjugated into fibrin during the polymerization process. NQEQVSP is valuable for research applications studying coagulation, fibrin formation, and related processes in hemostasis and thrombosis.
4-Methylumbelliferyl-β-D-glucuronide is a fluorogenic substrate utilized for the detection of β-glucuronidase activity. Upon enzymatic hydrolysis, it emits fluorescence at an excitation wavelength of 362 nm and an emission wavelength of 445 nm. This compound serves as an effective tool in research applications aimed at quantifying β-glucuronidase activity and monitoring Escherichia coli populations.
β-Secretase substrate VI, fluorogenic is a fluorogenic peptide labeled with EDANS and DABCYL, specifically designed for the measurement of β-site amyloid precursor protein cleaving enzyme 1 (BACE1) activity. This substrate enables the quantification of BACE1 enzymatic activity through fluorescence emission (Em=360nm, Ex=528nm), providing a direct correlation between enzyme activity levels and fluorescence intensity. It is an essential tool for researchers studying Alzheimer's disease and related amyloidogenic processes.
Boc-LRR-AMC is a fluorogenic substrate designed to detect the trypsin-like activity of both the 26S proteasome and the 20S proteasome core. Its highly sensitive fluorescence allows for precise measurement of proteasomal activity in various biological samples. Boc-LRR-AMC is valuable for research applications involving protein degradation, cellular regulation, and proteasome function assessment.
