S-Benzyl-L-cysteine 4-nitroanilide
Need Assistance?
  • US & Canada:
    +
  • UK: +

S-Benzyl-L-cysteine 4-nitroanilide

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

A substrate for cystyl aminopeptidase (oxytocinase).

Category
L-Amino Acids
Catalog number
BAT-004194
CAS number
7436-62-6
Molecular Formula
C16H17N3O3S
Molecular Weight
331.43
S-Benzyl-L-cysteine 4-nitroanilide
IUPAC Name
(2R)-2-amino-3-benzylsulfanyl-N-(4-nitrophenyl)propanamide
Synonyms
L-Cys(Bzl)-pNA
Appearance
Yellowish powder
Purity
≥ 98% (TLC)
Melting Point
99-102 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C16H17N3O3S/c17-15(11-23-10-12-4-2-1-3-5-12)16(20)18-13-6-8-14(9-7-13)19(21)22/h1-9,15H,10-11,17H2,(H,18,20)/t15-/m0/s1
InChI Key
HOZQMLJHNCMSRC-HNNXBMFYSA-N
Canonical SMILES
C1=CC=C(C=C1)CSCC(C(=O)NC2=CC=C(C=C2)[N+](=O)[O-])N

S-Benzyl-L-cysteine 4-nitroanilide, a specialized biochemical reagent, boasts a multitude of applications in research and diagnostics.

Enzyme Activity Assays: Serving as a crucial substrate in enzyme activity assays, S-Benzyl-L-cysteine 4-nitroanilide undergoes cleavage by proteases, yielding a measurable product that facilitates the quantification of enzyme activity. This method is indispensable for investigating the catalytic prowess of cysteine proteases in the domains of biochemical and pharmacological research, shedding intricate light on enzymatic mechanisms with finesse.

Drug Screening: In the realm of pharmaceutical exploration, S-Benzyl-L-cysteine 4-nitroanilide plays a vital role in high-throughput screening assays aimed at identifying potential protease inhibitors. By monitoring the enzymatic cleavage of this substrate, researchers can evaluate the efficacy of novel drug candidates, paving the path for the discovery and advancement of innovative therapeutics targeting protease-mediated pathways. This revolutionizes the landscape of drug development.

Biochemical Pathway Studies: Immersed in the intricate network of biochemical pathways involving cysteine proteases, researchers turn to S-Benzyl-L-cysteine 4-nitroanilide as a tool for unraveling the intricacies of regulatory mechanisms and interactions within these pathways. Through analyzing proteolytic cleavage patterns of this substrate, scientists extract invaluable insights into the inner workings of cellular processes and disease mechanisms, enriching our comprehension of the complexities governing biological systems.

Diagnostic Applications: Nestled within diagnostic kits, S-Benzyl-L-cysteine 4-nitroanilide emerges as a pivotal component for detecting the presence of cysteine proteases in biological samples. Its integration in colorimetric assays facilitates swift and straightforward identification of enzyme activity, serving as a crucial biomarker for a spectrum of diseases. This capability aids in the diagnosis and monitoring of conditions such as cancer and inflammatory diseases, providing a potent tool for healthcare professionals in their battle against these afflictions.

1. L-leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B
K Murata, Y Iba, Y Inoue, A Kimura Biochem Biophys Res Commun. 1988 Jun 16;153(2):767-72. doi: 10.1016/s0006-291x(88)81161-6.
An enzyme that catalyzes hydrolysis of S-benzyl-L-cysteine-p-nitroanilide was purified from E. coli B. The enzyme was a monomer with a molecular weight of 82,000. In addition to L-cysteinylglycine, the enzyme hydrolyzed various glycine-containing dipeptides most efficiently at pH 7.0. The enzyme required no metal ions for activity and was specifically inhibited by L-leucine and its analogue with free carboxyl group at the physiological concentrations.
Online Inquiry
Inquiry Basket