Suc-Ala-Glu-Pro-Phe-pNA (CAS 128802-76-6)
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Suc-Ala-Glu-Pro-Phe-pNA is a synthetic peptide utilized primarily as a chromogenic substrate in enzymatic assays to study the activity and specificity of proteases, particularly those involved in the cleavage of peptide bonds. This compound features a unique sequence of amino acids—Ala (Alanine), Glu (Glutamic acid), Pro (Proline), and Phe (Phenylalanine)—linked to a p-nitroanilide (pNA) group, which serves as a chromophore. Upon proteolytic cleavage, specifically at the Phe-pNA bond, the p-nitroaniline moiety is released, leading to a measurable increase in absorbance at a specific wavelength, typically around 405 nm. This property makes Suc-Ala-Glu-Pro-Phe-pNA an invaluable tool in biochemical research for quantifying protease activity, understanding protease specificity, and screening protease inhibitors. Its application extends across various fields, including enzymology, biochemistry, and molecular biology, facilitating insights into the mechanisms of action of proteases and their roles in physiological and pathological processes.
Suc-Ala-Glu-Pro-Phe-pNA (CAS 128802-76-6) References
- Deletion of various carboxy-terminal domains of Lactococcus lactis SK11 proteinase: effects on activity, specificity, and stability of the truncated enzyme. | Bruinenberg, PG., et al. 2000. Appl Environ Microbiol. 66: 2859-65. PMID: 10877779
- Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere. | Wang, XJ., et al. 2004. J Am Chem Soc. 126: 15533-42. PMID: 15563182
- The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils. | Shen, ZJ., et al. 2005. Nat Immunol. 6: 1280-7. PMID: 16273101
- Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. | Harrison, RK. and Stein, RL. 1990. Biochemistry. 29: 3813-6. PMID: 1693856
- Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1. | Daum, S., et al. 2006. Biochemistry. 45: 12125-35. PMID: 17002312
- Aryl indanyl ketones: efficient inhibitors of the human peptidyl prolyl cis/trans isomerase Pin1. | Daum, S., et al. 2006. Angew Chem Int Ed Engl. 45: 7454-8. PMID: 17048295
- Structural basis for high-affinity peptide inhibition of human Pin1. | Zhang, Y., et al. 2007. ACS Chem Biol. 2: 320-8. PMID: 17518432
- On the benefit of bivalency in peptide ligand/pin1 interactions. | Daum, S., et al. 2007. J Mol Biol. 374: 147-61. PMID: 17931657
- A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases. | Zoldák, G., et al. 2009. Biochemistry. 48: 10423-36. PMID: 19785464
- Pin1 and PKMzeta sequentially control dendritic protein synthesis. | Westmark, PR., et al. 2010. Sci Signal. 3: ra18. PMID: 20215645
- Theileria parasites secrete a prolyl isomerase to maintain host leukocyte transformation. | Marsolier, J., et al. 2015. Nature. 520: 378-82. PMID: 25624101
- A Selective, Cell-Permeable Nonphosphorylated Bicyclic Peptidyl Inhibitor against Peptidyl-Prolyl Isomerase Pin1. | Jiang, B. and Pei, D. 2015. J Med Chem. 58: 6306-12. PMID: 26196061
- Discovery of novel selenium derivatives as Pin1 inhibitors by high-throughput screening. | Subedi, A., et al. 2016. Biochem Biophys Res Commun. 474: 528-533. PMID: 27120460
- Imazamethabenz inhibits human breast cancer cell proliferation, migration and invasion via combination with Pin1. | Liu, C., et al. 2017. Mol Med Rep. 15: 3210-3214. PMID: 28350086
- Prolyl-Isomerase Pin1 Controls Key fMLP-Induced Neutrophil Functions. | Bedouhene, S., et al. 2021. Biomedicines. 9: PMID: 34572316
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Suc-Ala-Glu-Pro-Phe-pNA, 5 mg | sc-472004 | 5 mg | $200.00 |