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Merck

P5267

Sigma-Aldrich

L-Prolin-p-nitroanilid -trifluoracetat (Salz)

≥99% (TLC), suitable for ligand binding assays

Synonym(e):

N-(4-Nitrophenyl)pyrrolidine-2-carboxamide, P-pNA, Pro-pNA

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About This Item

Empirische Formel (Hill-System):
C11H13N3O3 · C2HF3O2
CAS-Nummer:
Molekulargewicht:
349.26
MDL-Nummer:
UNSPSC-Code:
12352209
eCl@ss:
32160406
PubChem Substanz-ID:
NACRES:
NA.26

Produktbezeichnung

L-Prolin-p-nitroanilid -trifluoracetat (Salz), prolyl aminopeptidase substrate

Qualitätsniveau

Assay

≥99% (TLC)

Form

powder

Methode(n)

ligand binding assay: suitable

Farbe

white to yellow

Lagertemp.

2-8°C

SMILES String

OC(=O)C(F)(F)F.[O-][N+](=O)c1ccc(NC(=O)[C@@H]2CCCN2)cc1

InChI

1S/C11H13N3O3.C2HF3O2/c15-11(10-2-1-7-12-10)13-8-3-5-9(6-4-8)14(16)17;3-2(4,5)1(6)7/h3-6,10,12H,1-2,7H2,(H,13,15);(H,6,7)/t10-;/m0./s1

InChIKey

KYRVEVYREUUAKH-PPHPATTJSA-N

Allgemeine Beschreibung

Proline p-nitroanilide (P-pNA) is a colorimetric substrate for prolyl aminopeptidase (proline iminopeptidase), an enzyme that releases proline from the N-terminus of small peptides.

Anwendung

L-Proline p-nitroanilide trifluoroacetate salt has also been used as a monopeptide substrate for measuring the amidolytic activity of fibrillated peptide catalyst, PC4.
Proline p-nitroanilide (P-pNA) has been used as a substrate for prolyl aminopeptidase (proline iminopeptidase) from cabbage leaves.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Hongyu Yang et al.
World journal of microbiology & biotechnology, 32(11), 176-176 (2016-09-16)
Prolyl aminopeptidases are specific exopeptidases that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. In the present study, the prolyl aminopeptidase gene (pap) from Aspergillus oryzae JN-412 was optimized through the codon usage of Pichia pastoris.
Margarita Marinova et al.
Protein and peptide letters, 16(2), 207-212 (2009-02-10)
Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and
Yoke-Ming Wong et al.
Biomacromolecules, 17(10), 3375-3385 (2016-09-20)
Amyloid fibers are classified as a new generation of tunable bionanomaterials that exhibit new functions related to their distinctive characteristics, such as their universality, tunability, and stiffness. Here, we introduce the catalytic residues of serine protease into a peptide catalyst
Paul J Lijnen et al.
Journal of the renin-angiotensin-aldosterone system : JRAAS, 6(2), 69-77 (2006-02-14)
To determine whether the aminopeptidase B inhibitor, arphamenine A, could affect collagen production and expression in control and TGF-ss1-treated cardiac fibroblasts. Cardiac fibroblasts from passage 2 from normal male adult rats were cultured to confluency and incubated with and without
Margarita Marinova et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 63(1-2), 105-112 (2008-04-05)
Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2-7.5 for aminopeptidase activity and 8.0-8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by

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