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P5267

Sigma-Aldrich

L-Proline p-nitroanilide trifluoroacetate salt

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

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):
C11H13N3O3 · C2HF3O2
CAS Number:
108321-19-3
Molecular Weight:
349.26
MDL number:
MFCD00069671
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
329820223
NACRES:
NA.26

product name

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

Assay

≥99% (TLC)

form

powder

technique(s)

ligand binding assay: suitable

color

white to yellow

storage temp.

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

InChI key

KYRVEVYREUUAKH-PPHPATTJSA-N

General description

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.

Application

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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.
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
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
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