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CAS 893-36-7

L-Leucine-2-naphthylamide Hydrochloride (2-Naphthylamine free) TCI L0037

L-Leucine-2-naphthylamide Hydrochloride (2-Naphthylamine free) TCI L0037

Chemical Identity

CAS No.
893-36-7
PubChem
CID 16219549·SID 87572005
Formula
C16H21ClN2O
Molecular weight
292.80 g/mol
Purity
>98.0%(HPLC)(T)
Reference databases
ChemSpider·ECHA
Full identifiers (IUPAC, SMILES, InChIKey)
IUPAC
(2S)-2-amino-4-methyl-N-naphthalen-2-ylpentanamide;hydrochloride
SMILES
CC(C)C[C@@H](C(=O)NC1=CC2=CC=CC=C2C=C1)N.Cl
InChIKey
HTHKKWZMEVJWQF-RSAXXLAASA-N
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L-Leucine-2-naphthylamide Hydrochloride is a chromogenic substrate developed specifically for measuring the activity of aminopeptidase enzymes, particularly leucine aminopeptidase. The molecule consists of an L-leucine residue bound to a 2-naphthylamine group through an amide linkage, and it is supplied as the hydrochloride salt to improve solubility and stability. When the enzyme cleaves the amide bond, the liberated naphthylamine group can be detected spectrophotometrically or through the formation of a coloured compound, allowing the rate of the enzymatic reaction to be followed quantitatively in biochemical studies and laboratory diagnostics.

The property that makes this substrate a preferred choice is its specificity toward aminopeptidases that cleave leucine residues at the amino terminus of a peptide chain, so that the measured result reflects the activity of the target enzyme with a low level of background interference. The "2-Naphthylamine free" designation in the product name indicates that the material has been prepared so that the free amine content is suppressed, which is important both for occupational safety and for measurement accuracy, since free amine can generate a background signal. The hydrochloride salt form supports the preparation of consistent assay solutions.

In Indonesian laboratories, this substrate is typically used in biochemistry and enzymology work where aminopeptidase activity must be quantified reliably. Its role in university research laboratories, clinical diagnostic support work, and enzyme characterisation studies rests on the same principle: a defined leucine-bearing substrate whose cleavage produces a readily measured signal. The hydrochloride form simplifies routine solution preparation, making the material practical for repeated assay runs across a working programme.

  • Leucine aminopeptidase activity assays, where the L-leucine residue at the amino terminus provides the specific cleavage point the enzyme recognises, giving a direct quantitative readout of enzyme activity.
  • General aminopeptidase enzymology studies, since the amide linkage to the 2-naphthylamine group releases a detectable chromogenic product whose formation rate can be followed spectrophotometrically over time.
  • Enzyme kinetics characterisation work, because the substrate delivers a reproducible signal that allows reaction rates to be measured quantitatively rather than estimated from indirect or endpoint observations alone.
  • Laboratory diagnostic support procedures, where aminopeptidase activity must be determined with low background interference thanks to the suppressed free 2-naphthylamine content of the preparation.
  • Biochemical method development and assay validation, as the hydrochloride salt form supports consistent preparation of test solutions across repeated runs and between different analytical sessions.

Brand TCI
CAS number 893-36-7
Molecular formula —
Purity —
Category Chemistry > Chemical Biology > Peptide Chemistry
Pack sizes please refer to the packaging options listed for this catalogue item
Physical form —
Storage store according to the manufacturer's stated conditions on the product label
  • Product code: L0037
  • Form: hydrochloride salt, prepared as 2-naphthylamine free

Store the material in its original tightly closed container under the conditions stated by the manufacturer on the product label, protected from moisture and kept away from incompatible substances. Suitable containers include the supplied amber or opaque chemical bottle, which limits light exposure and helps maintain the integrity of the substrate during storage. Handle the substance in a well-ventilated area or within a fume hood, wearing a laboratory coat, chemical-resistant gloves, and eye protection. Avoid the generation of dust when weighing, close the container promptly after use, and prepare working solutions only in clean labelled glassware. Dispose of residues and contaminated consumables through the laboratory's established chemical waste route.

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