Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

L1635

Sigma-Aldrich

L-Leucine β-naphthylamide

Synonym(s):

L-Leucine-2-naphthylamide

Sign Into View Organizational & Contract Pricing

Select a Size

100 MG
$57.80
1 G
$123.90

$57.80


Available to ship onMay 01, 2025Details



Select a Size

Change View
100 MG
$57.80
1 G
$123.90

About This Item

Empirical Formula (Hill Notation):
C16H20N2O
CAS Number:
Molecular Weight:
256.34
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.83

$57.80


Available to ship onMay 01, 2025Details


assay

≥98% (TLC)

Quality Level

form

powder

solubility

H2O: insoluble

storage temp.

−20°C

SMILES string

CC(C)C[C@H](N)C(=O)Nc1ccc2ccccc2c1

InChI

1S/C16H20N2O/c1-11(2)9-15(17)16(19)18-14-8-7-12-5-3-4-6-13(12)10-14/h3-8,10-11,15H,9,17H2,1-2H3,(H,18,19)/t15-/m0/s1

InChI key

JWHURRLUBVMKOT-HNNXBMFYSA-N

Looking for similar products? Visit Product Comparison Guide

Application

L-Leucine β-naphthylamide has been used as a substrate:
  • to measure the activity of aminopeptidase in Escherichia coli[1]
  • to evaluate the enzyme activity of cathepsin H from rabbit skeletal muscles[2]
  • in the proteolytic assay of L-Leucine aminopeptidase[3]

Substrate for leucine aminopeptidase determination in colorimetric and histochemical procedures.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Quality

Very low free β-naphthylamine.

Substrates

Substrate for aminopeptidase M

pictograms

Health hazard

signalword

Warning

hcodes

pcodes

Hazard Classifications

Carc. 2

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type P3 (EN 143) respirator cartridges


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

F Alba et al.
Life sciences, 43(11), 935-939 (1988-01-01)
Levels of soluble aminopeptidase (AP), measured as arylamidase activity using L-Leucine-2-Naphthylamide (Leu-2-NA) as substrate, were determined in the soluble fraction of eleven zones of rat brain. Results showed that AP activity is asymmetrically distributed in frontal cortex and hypothalamus with
J M de Gandarias et al.
Journal of biochemical toxicology, 7(3), 171-175 (1992-01-01)
Carbon disulfide, a volatile solvent, is widely used in industry. It has been demonstrated that it causes several neuropsychological symptoms. However, the neurochemical basis of its neurotoxic effect is relatively unknown. In this paper we have measured the effect of
A M Reisenauer et al.
Science (New York, N.Y.), 227(4682), 70-72 (1985-01-04)
The regulation of amino-oligopeptidase (AOP), an intestinal brush border hydrolase essential for the surface digestion of peptide nutrients, was examined in rats in vivo. Short-term (30-minute) intraintestinal perfusion of a tetrapeptide substrate, Gly-Leu-Gly-Gly, or a synthetic substrate, leucyl-beta-naphthylamide, induced a
Proteolytic activity in the placenta, decidua and postimplantation embryos of the rat.
A Fein et al.
Israel journal of medical sciences, 21(4), 394-396 (1985-04-01)
Masanori Matsuishi et al.
The international journal of biochemistry & cell biology, 35(4), 474-485 (2003-02-05)
Rabbit muscle cathepsin H classified as an aminoendopeptidase was purified and its properties were investigated to clarify its contribution to the proteolysis of postmortem muscle. The purification was performed by ammonium sulfate fractionation and successive chromatographies on Sephadex G-75, phosphocelluose

Questions

Reviews

No rating value

Active Filters

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service