Suc-Ala-Ala-Pro-Phe-pNA

Description:

A readily soluble, specific and sensitive substrate for chymotrypsin and human pancreatic elastase. It is also hydrolyzed by cathepsin G and chymase.

Sequence:

Succinylation-AAPF-p-Nitroanilide
  • General
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  • Name Suc-Ala-Ala-Pro-Phe-pNA
    Category Enzyme Substrates and Inhibitors
    One Letter Code Succinylation-AAPF-p-Nitroanilide
    Three Letter Code Succinylation-{Ala}{Ala}{Pro}{Phe}-p-Nitroanilide
    Molecular Weight 624.650
    Application Gastrointestinal Research
    Villmow, Marten, et al. "Inhibition of Aβ (1–40) fibril formation by cyclophilins." Biochemical Journal 473.10 (2016): 1355-1368.
    Küchler, Andreas, et al. "Stable and simple immobilization of proteinase K inside glass tubes and microfluidic channels." ACS applied materials & interfaces 7.46 (2015): 25970-25980.
    Munawar, Aisha, et al. "Elapid snake venom analyses show the specificity of the peptide composition at the level of genera Naja and Notechis." Toxins 6.3 (2014): 850-868.
    Weiss, André, David Kortemeier, and Jens Brockmeyer. "Biochemical characterization of the SPATE members EspPα and EspI." Toxins 6.9 (2014): 2719-2731.
    Herman, Julie, et al. "Der p 1 is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus." Biochimica et Biophysica Acta (BBA)-General Subjects 1840.3 (2014): 1117-1124.
    Jónsdóttir, Lilja B., et al. "The role of salt bridges on the temperature adaptation of aqualysin I, a thermostable subtilisin-like proteinase." Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1844.12 (2014): 2174-2181.
    Gogliettino, Marta, et al. "A novel class of bifunctional acylpeptide hydrolases–potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii." The FEBS journal 281.1 (2014): 401-415.
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