Suc-Ala-Ala-Pro-Leu-pNA

Description:

a sensitive substrate for human and especially porcine pancreatic elastases.

Sequence:

Succinylation-AAPL-p-Nitroanilide

General

References

Comments (0)

Name	Suc-Ala-Ala-Pro-Leu-pNA
Category	Enzyme Substrates and Inhibitors
One Letter Code	Succinylation-AAPL-p-Nitroanilide
Three Letter Code	Succinylation-{Ala}{Ala}{Pro}{Leu}-p-Nitroanilide
Molecular Weight	590.630
Application

Dotiwala, Farokh, et al. "A high yield and cost-efficient expression system of human granzymes in mammalian cells." JoVE (Journal of Visualized Experiments) 100 (2015): e52911.

Weiss, André, David Kortemeier, and Jens Brockmeyer. "Biochemical characterization of the SPATE members EspPα and EspI." Toxins 6.9 (2014): 2719-2731.

Weiss, Andre, Hanna Joerss, and Jens Brockmeyer. "Structural and functional characterization of cleavage and inactivation of human serine protease inhibitors by the bacterial SPATE protease EspPα from enterohemorrhagic E. coli." PloS one 9.10 (2014).

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.

Debowski, D., et al. "Hybrid analogues of SFTI‐1 modified in P1 position by β‐and γ‐amino acids and N‐substituted β‐alanines." Peptide Science 100.2 (2013): 154-159.

Karna, Natalia, et al. "Investigation of peptide splicing using two‐peptide‐chain analogs of trypsin inhibitor SFTI‐1." The FEBS journal 280.23 (2013): 6213-6222.