Succinyl-trialanine-4-nitroanilide is a chromogenic substrate incorporating a nitroaniline reporter for protease studies. The trialanine core provides a defined recognition sequence for cleavage-site analysis. Researchers employ it in kinetic assays, specificity mapping, and inhibitor evaluation. Its succinyl group improves solubility and substrate handling.
CAT No: R2249
CAS No:52299-14-6
Synonyms/Alias:SUC-ALA-ALA-ALA-PNA;52299-14-6;Succinyl-trialanine-4-nitroanilide;N-Succinyl-Ala-Ala-Ala-p-nitroanilide;9MJ6NSX3KJ;EINECS 257-823-5;Suc-AAA-pNA;Suc-Ala-Ala-Ala-p-nitroanilide;CHROMOZYM ELA;succinyl-L-trialanine p-nitroanilide;Trianiline-4-nitroanilide;Succinyl(Ala)3-p-nitroanilide;4-[[(2S)-1-[[(2S)-1-[[(2S)-1-(4-nitroanilino)-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;Succinyltrialanine-p-nitroanilide;DTXSID10200317;Succinyl-trialanine-p-nitroanilide;L-Alaninamide, N-(3-carboxy-1-oxopropyl)-L-alanyl-L-alanyl-N-(4-nitrophenyl)-;N-succinyl-L-trialanine p-nitroanilide;3-carboxypropionyl-trialanine-p-nitroanilide;Succinyl-alanyl-alanyl-alanine-p-nitroanilide;3-carboxypropionyl-alanyl-alanyl-alanyl-4-nitroanilide;SUCCINYL-L-ALANYL-L-ALANYL-L-ALANINE 4-NITROANILIDE;SUCCINYL-L-ALANYL-L-ALANYL-L-ALANYL P-NITROANILIDE;N-SUCCINYL-L-ALANYL-L-ALANYL-L-ALANINE P-NITROANILIDE;succinyl-Ala-Ala-Ala-p-nitroanilide;3-CARBOXYPROPIONYL-L-ALANYL-L-ALANYL-L-ALANINE P-NITROANILIDE;3-{[(1S)-1-{[(1S)-1-{[(1S)-1-[(4-NITROPHENYL)CARBAMOYL]ETHYL]CARBAMOYL}ETHYL]CARBAMOYL}ETHYL]CARBAMOYL}PROPANOIC ACID;4-(((S)-1-(((S)-1-(((S)-1-((4-Nitrophenyl)amino)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-4-oxobutanoic acid;UNII-9MJ6NSX3KJ;MFCD00036774;SLAPN;N-Succinyl-L-alanyl-L-alanyl-L-alanine 4-nitroanilide;suc(Ala)3-p-NA;Suc-Ala(3)-Nan;Suc-Ala(3)-NA;DTXCID10122808;GVUGADOWXGKRAE-SRVKXCTJSA-N;N-Suc-Ala-Ala-Ala-p-nitroanilide;succinyl-Ala-Ala-Ala p-nitroanilide;AKOS037645116;N-(3-Carboxypropionyl)-L-alanyl-L-alanyl-N-(p-nitrophenyl)-L-alaninamide;N-succinyl-Ala-Ala-Ala p-nitroanilide;succinyl-L-Ala-Ala-Ala-p-nitroanilide;FS46953;AS-57242;DA-67827;HY-137409;succinyl-L-Ala-L-Ala-L-Ala-p-nitroanilide;CS-0138485;NS00032474;F87971;succinyl-l-alanyl-l-alanyl-l-alanine p-nitroanilide;Q27272748;Elastase Substrate VIII, Colorimetric - CAS 52299-14-6;N-Succinyl-Ala-Ala-Ala-p-nitroanilide, elastase substrate;N-Succinyl-Ala-Ala-Ala p-nitroanilide; N-Succinyl-tri-L-alanine 4-nitroanilide;
Succinyl-trialanine-4-nitroanilide is a synthetic peptide substrate widely utilized in enzymology and biochemical research. Structurally, it consists of a succinylated tri-alanine peptide linked to a 4-nitroanilide chromophore, making it particularly valuable for quantitative enzyme assays. Its design enables researchers to investigate the activity and specificity of proteolytic enzymes, especially serine proteases such as elastase and chymotrypsin, through spectrophotometric detection. The chromogenic nature of the 4-nitroanilide moiety provides a convenient and sensitive readout, supporting detailed kinetic studies and mechanistic investigations in both academic and industrial settings.
Enzyme activity assays: A primary application of succinyl-trialanine-4-nitroanilide lies in the quantitative measurement of protease activity. Upon enzymatic cleavage by target proteases, the substrate releases 4-nitroaniline, which can be detected spectrophotometrically due to its characteristic absorbance. This property allows for real-time monitoring of enzyme kinetics, facilitating the determination of catalytic parameters such as Km and Vmax. Researchers rely on this substrate to screen for protease inhibitors, study enzyme specificity, and characterize mutant or engineered proteases, making it a cornerstone tool in enzymology.
Protease inhibitor screening: The substrate's well-defined cleavage site and chromogenic output render it highly suitable for high-throughput screening of protease inhibitors. By incorporating succinyl-trialanine-4-nitroanilide into assay platforms, scientists can rapidly evaluate the efficacy and selectivity of potential inhibitory compounds. The clear and quantifiable colorimetric response supports robust data collection and comparative analysis, accelerating the discovery and optimization of novel inhibitors for research and development purposes.
Enzyme specificity profiling: Succinyl-trialanine-4-nitroanilide serves as a model substrate for dissecting the substrate preferences of various serine proteases, particularly those with an affinity for small, neutral amino acid sequences. By comparing the rate and extent of hydrolysis across different enzymes, researchers can elucidate substrate recognition motifs and map the active site characteristics of proteolytic enzymes. Such insights are essential for understanding enzyme function, guiding rational protein engineering, and designing targeted substrates or inhibitors.
Biochemical pathway elucidation: The substrate's ability to report on protease activity supports broader investigations into proteolytic processing within complex biological samples. By applying succinyl-trialanine-4-nitroanilide in cell extracts or tissue homogenates, scientists can monitor the activity of endogenous proteases under various experimental conditions. This approach aids in unraveling regulatory mechanisms, post-translational modifications, and the dynamic roles of proteases in physiological and pathological processes.
Analytical method development: The reliable and reproducible chromogenic response of succinyl-trialanine-4-nitroanilide makes it a valuable standard in the development and validation of analytical methods for enzyme quantification. Laboratories employ this substrate to calibrate assay systems, optimize detection parameters, and establish reference protocols for routine protease analysis. Its consistent performance enhances assay reproducibility and supports quality control in both basic research and industrial applications.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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