118969-27-0

Basic information

• Product Name: 4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID
• Synonyms: ADL;6-AMINO-6-DEOXYLUCIFERIN;6-AMINO-D-LUCIFERIN;6-AMINO LUCIFERIN;4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID;6-AMINO-6-DEOXYLUCIFERIN (ADL);6-AMino-6-deoxyluciferin (D-isoMer);2-(6-AMinobenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid
• CAS NO: 118969-27-0
• Molecular Formula: C₁₁H₉N₃O₂S₂
• Molecular Weight: 279.34
• Mol File: 118969-27-0.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 594.9°Cat760mmHg
• Flash Point: 313.6°C
• Appearance: /
• Density: 1.81g/cm³
• Vapor Pressure: 5.33E-15mmHg at 25°C
• Refractive Index: 1.887
• PKA: 3.47±0.20(Predicted)
• CAS DataBase Reference: 4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID(118969-27-0)
• EPA Substance Registry System: 4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID(118969-27-0)

Safety Data

• Hazardous Substances Data: 118969-27-0(Hazardous Substances Data)

Usage

General Description

4,5-Dihydro-2[6-amino-2-benzthiazolyl]-4-thiazole carboxylic acid is a chemical compound with the molecular formula C11H10N4OS3. It is a heterocyclic compound that contains both thiazole and benzothiazole rings, as well as an amino group and a carboxylic acid functional group. 4,5-DIHYDRO-2[6-AMINO-2-BENZTHIAZOLYL]-4-THIAZOLE CARBOXYLIC ACID may have potential pharmaceutical or biological applications due to its unique structure and properties. Further research and studies may be needed to fully understand the potential uses and effects of this chemical.

InChI:InChI=1/C11H9N3O2S2/c12-5-1-2-6-8(3-5)18-10(13-6)9-14-7(4-17-9)11(15)16/h1-3,7H,4,12H2,(H,15,16)

Upstream product

• 7724-12-1 2-cyano-6-aminobenzothiazole 
• 921-01-7 rac-cysteine 
• 32443-99-5 D-cysteine hydrochloride 
• 2406-90-8 2-chlorobenzothiazol-6-ylamine 

Relevant articles and documents

A Bioluminogenic Probe for Monitoring Tyrosinase Activity

A bioluminogenic probe based on luciferin was designed and synthesized to monitor tyrosinase activity. This probe was efficient in assessing tyrosinase activity in a buffered aqueous solution and in measuring endogenous tyrosinase activity in melanoma cel

Mechanistic study of CBT-Cys click reaction and its application for identifying bioactive N-terminal cysteine peptides in amniotic fluid

CBT-Cys click condensation reaction has a high second-order reaction rate constant and has found wide applicability in recent years. However, its reaction mechanism has not been experimentally validated and its application for identifying bioactive N-terminal Cys peptides in real clinical samples has not been reported. Herein, firstly, by employing induced nanoelectrospray ionization-mass spectrometry (InESI-MS) and a home-built micro-reactor, we successfully intercepted and structurally characterized the crucial intermediate in this click reaction for the first time. With the intermediate, the proposed mechanism of this reaction was corroborated. Moreover, we also applied this MS setup to monitor the reaction in real time and obtained the second-order reaction rate constants of this reaction at different pH values. After mechanistic study, we applied this click reaction for identifying bioactive N-terminal cysteine peptides in amniotic fluid (AF). Eight unique N-terminal Cys peptides in AF, three of which are located in the functional domain regions of their corresponding proteins, were identified with a false positive rate less than 1%. One of the three peptides was found able to inhibit the growth of uterine endometrial cancer HEC-1-B cells but not the endometrial normal cells via a typical apoptotic pathway. With its mechanism satisfactorily elucidated, the kinetic parameters obtained, as well as its application for fishing bioactive N-terminal Cys peptides from vast complex clinical samples, we anticipate that this CBT-Cys click reaction could be applied more widely for the facile isolation, site-specific identification, and quantification of N-terminal Cys-containing peptides in complex biological samples.