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L7002

L-Lysine p-nitroanilide dihydrobromide

Name: <SC>L</SC>-Lysine p-nitroanilide dihydrobromide
Brand: SIGMA

≥98% (TLC), suitable for ligand binding assays

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About This Item

Empirical Formula (Hill Notation):

C₁₂H₁₈N₄O₃ · 2HBr

CAS Number:

40492-96-4

Molecular Weight:

428.12

MDL number:

MFCD00050686

UNSPSC Code:

12352209

PubChem Substance ID:

24896389

NACRES:

NA.26

product name

L-Lysine p-nitroanilide dihydrobromide,

Assay

≥98% (TLC)

Quality Level

200

form

powder

technique(s)

ligand binding assay: suitable

color

white to off-white

storage temp.

2-8°C

SMILES string

Br.NCCCC[C@H](N)C(=O)Nc1ccc(cc1)N(=O)=O

InChI

1S/C12H18N4O3.BrH/c13-8-2-1-3-11(14)12(17)15-9-4-6-10(7-5-9)16(18)19;/h4-7,11H,1-3,8,13-14H2,(H,15,17);1H/t11-;/m0./s1

InChI key

FJNCJWJSSUJZMS-MERQFXBCSA-N

Related Categories

Amino Acids

Application

L-Lysine p-nitroanilide may be used as a substrate to study the specificity and kinetics of lysine aminopeptidase(s) and various proteinases.

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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Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae.

Natasa Bozić et al.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 134(2), 231-241 (2003-02-06)

Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH

Purification and characterization of a lysine aminopeptidase from Kluyveromyces marxianus.

Bernardo Ramírez-Zavala et al.

FEMS microbiology letters, 235(2), 369-375 (2004-06-09)

A lysine aminopeptidase was purified from the yeast Kluyveromyces marxianus. This enzyme was purified 100-fold from a soluble extract obtained at 100,000g. The purification procedure consisted in fractionated precipitation with ammonium sulfate and five chromatography steps. The native enzyme had

Acceleration of enzymatic reaction of trypsin through the formation of water-soluble complexes with poly(ethylene glycol)-block-poly(alpha,beta-aspartic acid).

Akifumi Kawamura et al.

Biomacromolecules, 6(2), 627-631 (2005-03-15)

The amidase activity of bovine pancreas trypsin in water-soluble complexes with poly(ethylene glycol)-block-poly(alpha,beta-aspartic acid) (PEG-PAA) was evaluated by a colorimetric assay using L-lysine p-nitroanilide as a substrate. The enzymatic reaction of trypsin was accelerated through the complexation with PEG-PAA. By

Deletion of a conserved transcript PG_RS02100 expressed during logarithmic growth in Porphyromonas gingivalis results in hyperpigmentation and increased tolerance to oxidative stress.

Priscilla L Phillips et al.

PloS one, 13(11), e0207295-e0207295 (2018-11-13)

The oral obligate anaerobe Porphyromonas gingivalis possesses a small conserved transcript PG_RS02100 of unknown function we previously identified using small RNA-seq analysis as expressed during logarithmic growth. In this study, we sought to determine if PG_RS02100 plays a role in

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