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P5267

Sigma-Aldrich

L-Proline p-nitroanilide trifluoroacetate salt

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

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C11H13N3O3 · C2HF3O2
Número de CAS:
108321-19-3
Peso molecular:
349.26
Número MDL:
MFCD00069671
Código UNSPSC:
12352209
eCl@ss:
32160406
ID de la sustancia en PubChem:
329820223
NACRES:
NA.26

product name

L-Proline p-nitroanilide trifluoroacetate salt, prolyl aminopeptidase substrate

Análisis

≥99% (TLC)

formulario

powder

técnicas

ligand binding assay: suitable

color

white to yellow

temp. de almacenamiento

2-8°C

cadena SMILES

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

Clave InChI

KYRVEVYREUUAKH-PPHPATTJSA-N

Categorías relacionadas

Descripción general

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.

Aplicación

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Kazuyuki Hiwatashi et al.
Bioscience, biotechnology, and biochemistry, 68(6), 1395-1397 (2004-06-25)
We have found a novel prolyl aminopeptidase in Grifola frondosa. The enzyme was purified by DEAE-Sepharose CL-6B, Butyl-Toyopearl, Sephacryl S-100, and Mono-Q column chromatographies. The purified enzyme exists as a dimer and gives high activity toward L-proline-p-nitroanilide. The enzyme was
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.
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
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.
Cathal S Mahon et al.
Microbiology (Reading, England), 155(Pt 11), 3673-3682 (2009-06-27)
Fungi are capable of degrading proteins in their environment by secreting peptidases. However, the link between extracellular digestion and intracellular proteolysis has scarcely been investigated. Mycelial lysates of the filamentous fungus Talaromyces emersonii were screened for intracellular peptidase production. Five
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