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, also known as Suc-Ala3-pNA, is a synthetic chromogenic substrate widely recognized for its utility in biochemical and enzymological research. Characterized by its stable peptide sequence linked to a 4-nitroaniline group, this compound offers a reliable means of detecting and quantifying specific protease activities, particularly those involving serine proteases. Upon enzymatic cleavage, the release of 4-nitroaniline yields a distinct colorimetric change, enabling straightforward spectrophotometric analysis. Its well-defined structure and predictable reactivity make it a preferred choice for experimental systems requiring precise substrate specificity and reproducible results.
Protease Activity Assays: Succinyl-trialanine-4-nitroanilide is extensively used in the assessment of protease activity, especially for enzymes such as elastase and chymotrypsin-like serine proteases. By incorporating the substrate into enzymatic assays, researchers can monitor the hydrolysis of the peptide bond, which liberates the chromogenic p-nitroaniline moiety. The resultant color change, quantifiable at 405 nm, facilitates kinetic studies and inhibitor screening, providing valuable insights into enzyme specificity, catalytic efficiency, and mechanistic properties. This approach is indispensable for characterizing novel proteases and validating the selectivity of protease inhibitors in vitro.
Enzyme Kinetics and Mechanistic Studies: Suc-Ala3-pNA serves as a fundamental tool for detailed kinetic analyses of proteolytic enzymes. Its defined peptide sequence allows for the systematic investigation of substrate preferences and turnover rates, supporting the elucidation of catalytic mechanisms. By varying substrate concentrations and monitoring reaction velocities, scientists can derive Michaelis-Menten parameters and determine the effects of mutations or chemical modifications on enzyme function. Such studies are critical for advancing the understanding of protease regulation and for informing the rational design of enzyme modulators.
High-Throughput Screening: The chromogenic nature of succinyl-trialanine-4-nitroanilide lends itself to high-throughput screening platforms, where rapid and parallel assessment of protease activity is required. Automated liquid handling systems can efficiently dispense the substrate across microplate formats, enabling the evaluation of large compound libraries for potential protease inhibitors or activators. The direct, colorimetric readout streamlines data acquisition and analysis, making it an ideal substrate for drug discovery programs and functional genomics applications targeting proteolytic pathways.
Quality Control and Enzyme Production: In industrial and research settings, Suc-Ala3-pNA is employed for quality control during the production and purification of proteolytic enzymes. By incorporating the substrate into routine assays, manufacturers and laboratories can verify enzyme potency, stability, and batch-to-batch consistency. The reproducible colorimetric response provides a straightforward metric for monitoring enzyme activity over time, ensuring that products meet functional requirements for downstream applications in biotechnology, diagnostics, or basic research.
Biochemical Education and Training: Succinyl-trialanine-4-nitroanilide is also valuable in educational environments, where it serves as a demonstrative substrate for teaching fundamental concepts in enzymology and protein chemistry. Its visible color change upon enzymatic cleavage offers a tangible, real-time illustration of enzyme-substrate interactions, making it suitable for laboratory courses and training workshops. By enabling hands-on experience with enzyme assays, it helps students and trainees develop practical skills in experimental design, data interpretation, and quantitative analysis, fostering a deeper understanding of proteolytic mechanisms and assay development.
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