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H-Gly-L-Arg-pNA*2HCl
Nom chimique: Glycyl-L-arginine p-nitroanilide dihydrochloride // Synonymes: H-Gly-Arg-pNA*2HCl
- n° Art.:HAA2755
- n° CAS:103192-40-1 net
- Formule:C14H21N7O4*2HCl
- Masse moléculaire:351,36*72,9 g/mol
- Pureté:min. 98%
- Pureté Énantiomérique:min. 99,7%
Starting at 120,00 €
description
Gly-L-Arg-pNA is a chromgenic substrate for Dipeptiylpeptidase I (DPP I; cathepsin C) and DPP II or P. gingivalis dipeptidyl peptidase. It can furthermore be used as building block for test substrates for Coagulation Factor Xa and XIIa, t-Plasminogen Activator (tPAS) and u-Plasminogen Activator (uPA), Envelysin, C1 Esterase Inhibitor, Trypsin, Matriptase, horseshoe crab clotting enzyme and many others.
references
1. Dipeptidyl peptidase with strict substrate specificity of an anaerobic periodontopathogen Porphyromonas gingivalis; S. Fujimura, K. Hirai and Y. Shibata; FEMS Microbiol Lett 2002; 209: 127-31.
2. The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C); D. W. Hutchinson and A. Tunnicliffe; Biochim Biophys Acta 1987; 916: 1-4.
3. Human tissue factor pathway inhibitor fused to CD4 binds both FXa and TF/FVIIa at the cell surface; K. Riesbeck, A. Dorling, G. Kemball-Cook, J. H. McVey, M. Jones, E. G. Tuddenham and R. I. Lechler; Thromb Haemost 1997; 78: 1488-94.
4. Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop; K. Sichler, E. Kopetzki, R. Huber, W. Bode, K. P. Hopfner and H. Brandstetter; J Biol Chem 2003; 278: 4121-6.
5. Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors; M. Renatus, W. Bode, R. Huber, J. Sturzebecher, D. Prasa, S. Fischer, U. Kohnert and M. T. Stubbs; J Biol Chem 1997; 272: 21713-9.
6. Current diagnostic possibilities in hereditary angioedema and acquired angioedema; W. Dick and W. Cullmann; Immun Infekt 1985; 13: 113-8.
7. Chromogenic substrates for horseshoe crab clotting enzyme. Its application for the assay of bacterial endotoxins; S. Iwanaga, T. Morita, T. Harada, S. Nakamura, M. Niwa, K. Takada, T. Kimura and S. Sakakibara; Haemostasis 1978; 7: 183-8.
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