Fluorogenic Substrates

Chymotrypsin Substrate II, Fluorogenic is a specialized fluorogenic substrate designed to exhibit enhanced fluorescence upon cleavage by chymotrypsin. Its unique peptide sequence facilitates specific interactions with the enzyme, leading to a measurable increase in fluorescence intensity. This substrate demonstrates rapid turnover rates, allowing for real-time monitoring of proteolytic activity. The compound's distinct spectral properties enable sensitive detection in complex biological systems, making it an effective tool for studying enzymatic dynamics.

Resorufin benzyl ether is a fluorogenic compound that exhibits a remarkable increase in fluorescence upon enzymatic hydrolysis. Its structure allows for specific interactions with various hydrolases, resulting in a swift release of resorufin, which is characterized by its vibrant emission. The compound's unique electron-donating benzyl group enhances its photophysical properties, enabling sensitive detection in diverse environments. Its reaction kinetics are influenced by substrate concentration and enzyme specificity, making it a versatile tool for probing enzymatic mechanisms.

Ac-YVAD-AFC is a fluorogenic substrate that demonstrates a significant fluorescence enhancement upon cleavage by caspases. Its design incorporates a peptide sequence that selectively interacts with these proteases, facilitating rapid hydrolysis. The resulting release of AFC (7-amino-4-trifluoromethylcoumarin) leads to a pronounced fluorescence signal. This compound's unique structural features and reaction kinetics allow for precise monitoring of caspase activity, making it an effective probe for studying apoptotic pathways.

Ac-YEVD-AMC is a fluorogenic substrate characterized by its selective cleavage by caspases, leading to a notable increase in fluorescence. The compound features a unique peptide sequence that engages specifically with caspase enzymes, promoting efficient hydrolysis. Upon cleavage, the release of AMC (7-amino-4-methylcoumarin) generates a strong fluorescent signal. Its distinct molecular interactions and rapid reaction kinetics enable detailed analysis of proteolytic activity, providing insights into cellular processes.

4-Methylumbelliferyl-β-D-glucopyranoside is a fluorogenic compound that exhibits remarkable specificity for β-glucosidases. Upon enzymatic hydrolysis, it releases 4-methylumbelliferone, which emits strong fluorescence, facilitating sensitive detection. The compound's structure allows for effective substrate-enzyme interactions, enhancing reaction rates. Its unique properties make it an excellent tool for studying glycosidase activity and understanding carbohydrate metabolism dynamics.

Ac-VAD-AFC is a fluorogenic substrate that selectively targets caspases, key enzymes in apoptosis. Upon cleavage, it releases a highly fluorescent product, enabling real-time monitoring of caspase activity. The compound's design incorporates a peptide sequence that mimics natural substrates, promoting efficient enzyme binding and catalysis. Its rapid reaction kinetics and high sensitivity make it an essential tool for investigating cellular apoptosis pathways and proteolytic processes.

Proteasome Substrate I is a fluorogenic compound that serves as a substrate for proteasomes, facilitating the study of protein degradation pathways. Upon proteolytic cleavage, it emits a bright fluorescent signal, allowing for the quantification of proteasome activity. Its unique peptide structure enhances specificity for proteasomal enzymes, while the rapid turnover rate ensures timely detection of proteolytic events, making it a powerful tool for exploring cellular protein dynamics.

Ac-VDVAD-AFC is a fluorogenic substrate designed to selectively interact with specific proteolytic enzymes. Its unique peptide sequence promotes high affinity binding, enabling precise monitoring of protease activity. The compound exhibits rapid fluorescence enhancement upon cleavage, allowing for real-time tracking of enzymatic reactions. This dynamic behavior, coupled with its tailored molecular interactions, makes it an effective probe for dissecting proteolytic pathways in various biological contexts.

Resorufin butyrate is a fluorogenic compound characterized by its ability to undergo significant fluorescence enhancement upon enzymatic hydrolysis. Its unique structure facilitates interactions with hydrolases, leading to a rapid release of resorufin, a highly fluorescent product. The compound's reaction kinetics are influenced by the steric and electronic properties of the butyrate moiety, allowing for sensitive detection of enzymatic activity in diverse biochemical environments.

Glutaryl-L-phenylalanine 7-amido-4-methylcoumarin is a fluorogenic substrate that exhibits remarkable fluorescence upon enzymatic cleavage. Its design incorporates a coumarin moiety, which enhances light emission through intramolecular interactions. The compound's unique structure allows for selective binding to specific enzymes, resulting in a rapid and measurable fluorescence response. The reaction kinetics are finely tuned by the glutaryl and phenylalanine components, enabling precise monitoring of enzymatic processes.