Date published: 2025-10-3

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Trypsin Substrates

Santa Cruz Biotechnology now offers a broad range of Trypsin Substrates for use in various applications. Trypsin substrates are essential biochemical tools used extensively in proteomics and enzyme kinetics studies. These substrates facilitate the study of protease activity, specifically trypsin, a serine protease enzyme that cleaves peptide bonds in proteins. In research laboratories, trypsin substrates are crucial for investigating protein structure and function, understanding enzymatic pathways, and developing assays to measure enzyme activity. They enable scientists to probe the specificity of trypsin and other proteases, providing insights into protein digestion and processing. Additionally, trypsin substrates are used in the purification and preparation of proteins, as they assist in the controlled cleavage of fusion proteins and the removal of tags. This versatility makes them indispensable in molecular biology, biochemistry, and cell biology research. With a broad selection of synthetic and natural substrates, researchers can choose the most suitable one for their specific experimental needs, whether for qualitative analysis or quantitative measurements. View detailed information on our available Trypsin Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

L-Arginine 7-amido-4- methylcoumarin dihydrochloride

113712-08-6sc-281539
sc-281539A
100 mg
250 mg
$136.00
$238.00
(0)

L-Arginine 7-amido-4-methylcoumarin dihydrochloride serves as a substrate for trypsin, showcasing unique fluorescence properties upon enzymatic cleavage. Its structure allows for specific interactions with the active site of trypsin, leading to efficient hydrolysis. The compound exhibits distinct reaction kinetics, with a measurable increase in fluorescence intensity correlating with substrate conversion. This behavior highlights its potential for real-time monitoring of proteolytic activity in biochemical assays.

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride

21653-40-7sc-253173
sc-253173A
25 mg
100 mg
$82.00
$230.00
(0)

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride acts as a selective substrate for trypsin, characterized by its unique chromogenic properties. Upon cleavage by trypsin, it releases a nitroaniline moiety, resulting in a colorimetric change that can be quantitatively analyzed. The compound's structural features facilitate strong binding to the enzyme's active site, enhancing reaction rates. Its distinct kinetic profile allows for precise measurement of trypsin activity in various experimental conditions.

Nα-Benzoyl-DL-arginine β-naphthylamide hydrochloride

913-04-2sc-250547
sc-250547A
500 mg
1 g
$68.00
$98.00
(0)

Nα-Benzoyl-DL-arginine β-naphthylamide hydrochloride serves as a specific substrate for trypsin, exhibiting unique fluorescence properties upon enzymatic cleavage. The β-naphthylamide group enhances the compound's affinity for the enzyme, promoting efficient substrate-enzyme interactions. This compound's reaction kinetics reveal a rapid turnover rate, making it suitable for dynamic studies of proteolytic activity. Its structural design allows for selective recognition by trypsin, facilitating detailed enzymatic analysis.

N-4-Tosyl-L-arginine methyl ester hydrochloride

1784-03-8sc-207949
sc-207949A
5 g
25 g
$40.00
$118.00
1
(0)

N-4-Tosyl-L-arginine methyl ester hydrochloride acts as a potent trypsin substrate, characterized by its sulfonamide moiety that enhances binding affinity through specific electrostatic interactions. The compound's unique structure promotes a favorable transition state during hydrolysis, resulting in distinct reaction kinetics. Its hydrophobic characteristics contribute to solubility in various environments, allowing for versatile experimental applications in protease activity assessments.

N-α-Benzoyl-L-arginine ethyl ester hydrochloride

2645-08-1sc-269942
1 g
$36.00
(0)

N-α-Benzoyl-L-arginine ethyl ester hydrochloride serves as a selective substrate for trypsin, distinguished by its aromatic benzoyl group that facilitates strong π-π stacking interactions with the enzyme's active site. This compound exhibits unique reaction kinetics, characterized by a rapid cleavage rate due to its optimal steric configuration. Additionally, its ethyl ester functionality enhances lipophilicity, promoting effective substrate-enzyme interactions in diverse biochemical assays.

Nα-Benzoyl-L-arginine-7-amido-4-methylcoumarin hydrochloride

83701-04-6sc-301455
sc-301455A
50 mg
250 mg
$130.00
$531.00
2
(0)

Nα-Benzoyl-L-arginine-7-amido-4-methylcoumarin hydrochloride acts as a specific substrate for trypsin, featuring a coumarin moiety that fluoresces upon cleavage, allowing for real-time monitoring of enzymatic activity. The compound's unique amide bond enhances its stability while facilitating precise interactions with the enzyme's active site. Its distinct structural design promotes efficient hydrolysis, making it a valuable tool for studying proteolytic pathways and enzyme kinetics.

N-α-Benzoyl-DL-arginine 4-nitroanilide monohydrochloride

911-77-3sc-207952
sc-207952A
sc-207952B
100 mg
500 mg
5 g
$67.00
$79.00
$292.00
(0)

N-α-Benzoyl-DL-arginine 4-nitroanilide monohydrochloride serves as a selective substrate for trypsin, characterized by its nitroanilide group that undergoes significant colorimetric changes upon enzymatic cleavage. This transformation allows for quantitative analysis of trypsin activity. The compound's unique structural features, including the aromatic benzoyl group, enhance its binding affinity to the enzyme, promoting rapid reaction kinetics and facilitating detailed studies of proteolytic mechanisms.

Nα-Benzoyl-L-arginine 4-methoxy-β-naphthylamide hydrochloride

100900-33-2sc-215529
sc-215529A
sc-215529B
25 mg
50 mg
250 mg
$214.00
$306.00
$510.00
1
(0)

Nα-Benzoyl-L-arginine 4-methoxy-β-naphthylamide hydrochloride acts as a specific substrate for trypsin, distinguished by its methoxy-β-naphthylamide moiety, which exhibits notable fluorescence changes upon enzymatic hydrolysis. This property enables sensitive detection of trypsin activity. The compound's unique interactions with the enzyme's active site, driven by its aromatic and polar characteristics, enhance substrate specificity and influence reaction rates, providing insights into proteolytic pathways.