Chinese Name: MeO-Suc-Arg-Pro-Tyr-pNA

English Name: MeO-Suc-Arg-Pro-Tyr-pNA

Abbreviation: S-2586

CAS Number: 82564-18-9

Molecular Formula: C31H40N8O9

Molecular Weight: 668.71

Specifications: 25 mg / 500 mg / 1 g (Custom packaging supported)

Form: Off-white crystalline powder

Product Number: G04010023

Stock: In stock

Color Signal: Yellow absorption at 405 nm

Chinese Name: MeO-Suc-Arg-Pro-Tyr-pNA · HCl

English Name: MeO-Suc-Arg-Pro-Tyr-pNA · HCl

Abbreviation: S-2586

CAS Number: 86170-42-5

Molecular Formula: C31H41ClN8O9

Molecular Weight: 705.17

Specifications: 25 mg / 500 mg / 1 g (Custom packaging supported)

Form: Off-white crystalline powder

Product Number: G04010022

Stock: In stock

Color Signal: Yellow absorption at 405 nm

The molecular structure of S-2586 (MeO-Suc-Arg-Pro-Tyr-pNA) consists of two parts: the "substrate recognition sequence" and the "chromogenic signal group":

• Recognition end: MeO-Suc-Arg-Pro-Tyr peptide sequence, where the peptide bond between Tyr and pNA is the cleavage site for chymotrypsin and its homologous enzymes (such as kallikrein, chymase). The enzyme specifically hydrolyzes at this site.

• Signal end: pNA (p-nitroaniline) is attached as a chromogenic group at the terminus of the substrate. When bound to the peptide chain, its absorption at 405 nm is weak. Once cleaved and released as a free state, free pNA produces a significant absorption signal at 405 nm, turning the solution yellow, with the signal proportional to enzyme activity.

Reaction chain:
Chymotrypsin → Cleaves Tyr-pNA bond → Release of free pNA → Increase in absorbance at 405 nm → Darker color, stronger enzyme activity.

During this reaction, the rate of pNA release is directly related to chymotrypsin activity. Therefore, it can be used for continuous enzyme kinetic monitoring, substrate specificity analysis, and inhibitor evaluation experiments.

1. Chymotrypsin activity detection

Used to establish a continuous chromogenic detection system for chymotrypsin, monitoring enzyme activity levels by measuring absorbance changes at 405 nm. Suitable for:

• Quantitative analysis of enzyme activity;

• Continuous kinetic detection;

• Comparison of enzyme activity under different experimental conditions;

2. Study of substrate recognition by serine proteases

Using substrate sequences containing aromatic amino acid sites to study the recognition and cleavage preference of chymotrypsin for substrates. Helps in:

• Substrate selectivity studies;

• Analysis of cleavage mechanisms;

• Optimization of sequence structure;

3. Protease inhibitor screening and kinetic studies

By monitoring the change in pNA release rate, it can be used to evaluate the activity of candidate inhibitors and study kinetic parameters such as Km and Vmax. Helps in:

• Establishing a continuous kinetic evaluation system;

• Improving inhibitor screening efficiency;

• Reducing the impact of endpoint assay errors;

✅ High purity, low background interference

High-purity peptide synthesis and rigorous purification processes help reduce background absorption interference caused by free pNA and degradation impurities. In low-activity detection and continuous kinetic experiments, this improves data stability and signal-to-noise ratio in the low OD range.

✅ Sequence design tailored to chymotrypsin recognition characteristics

Based on chymotrypsin's cleavage preference for aromatic amino acid residues, the product adopts a peptide sequence containing a Tyr site. It can be used to establish targeted enzyme activity detection and continuous kinetic analysis systems, making it more suitable for substrate specificity analysis and cleavage mechanism studies.

✅ Continuous color development, more intuitive kinetic monitoring

Based on the classic pNA release mechanism, the cleavage process can be continuously recorded by measuring absorbance changes at 405 nm. Compared to simple endpoint detection, this is more suitable for Km/Vmax analysis, inhibitor evaluation, and studying the enzymatic reaction process.

✅ Multiple salt forms available, flexible adaptation to experimental systems

The hydrochloride salt can be directly dissolved in aqueous buffers, avoiding DMSO interference. The free base is the classic form found in the literature, suitable for DMSO-assisted dissolution procedures. Users can freely choose the desired salt form according to their experimental system, and Hepattack Bioscience & Technology supports customization on demand.

✅ High compatibility of pNA system, easier method establishment

Compared to some fluorescence detection systems that rely on complex filter modules, pNA chromogenic substrates have higher compatibility with standard microplate readers, requiring no additional fluorescence detection configurations. They are more suitable for standardized enzymatic experiments and method establishment in routine laboratories.

✅ In-stock supply, reducing experiment waiting time

We offer in-stock supply of multiple specifications: 25 mg, 500 mg, and 1 g, and support custom packaging. This better meets the needs of continuous research projects, pilot validation, and long-term experimental planning.