41994-02-9

Usage

Uses

Used in Pharmaceutical Industry:
1H-Thieno[3,4-d]iMidazole-4-pentanaMide, hexahydro-N-[2-(4-hydroxyphenyl)ethyl]-2-oxo-, (3aS,4S,6aR)is used as a pharmaceutical intermediate for the development of new drugs. Its unique structure and functional groups make it a promising candidate for the synthesis of various therapeutic agents.
Used in Chemical Research:
1H-Thieno[3,4-d]iMidazole-4-pentanaMide, hexahydro-N-[2-(4-hydroxyphenyl)ethyl]-2-oxo-, (3aS,4S,6aR)is used as a research tool in chemical laboratories to study its properties, reactivity, and potential applications. Its unique structure allows researchers to explore new synthetic routes and investigate its interactions with other molecules.
Used in Material Science:
1H-Thieno[3,4-d]iMidazole-4-pentanaMide, hexahydro-N-[2-(4-hydroxyphenyl)ethyl]-2-oxo-, (3aS,4S,6aR)can be used in the development of new materials with specific properties. Its unique structure and functional groups can be exploited to create materials with tailored characteristics for various applications.

References

1) Bobrow?et al.?(1989),?Catalyzed reporter deposition, a novel method of signal amplification. Application to immunoassays; J. Immunol. Methods,?125?279 2) Evans?et al.?(2003),?Optimization of biotinyl-tyramide-based in situ hybridization for sensitive background-free applications in formalin-fixed, paraffin-embedded tissue specimens; BMC. Clin. Pathol.,?3?2 3) Draerova?et al.?(2013),?Quantification of a-tubulin by sandwich ELISA with signal amplification through niotinyl-tyramide or immune-PCR; J. Immunol. Methods,?395?63 4) Einarson and Sen (2017),?Self-biotinylation of DNA G-quadruplexes via intrinsic peroxidase activity; Nucleic Acids Res.,?45?9813 5) Hwang and Espenshade (2016),?Proximity-dependent biotin labelling in yeast using the engineered ascorbate peroxidase APEX2; Biochem. J.,?473?2463

Upstream product

• 58-85-5 biotin 
• 51-67-2 tyrosamine 
• 35013-72-0 biotin N-Hydroxysuccinimide ester 

Relevant academic research and scientific papers

Enzymatic Modification of N-Terminal Proline Residues Using Phenol Derivatives

A convenient enzymatic strategy is reported for the modification of proline residues in the N-terminal positions of proteins. Using a tyrosinase enzyme isolated from Agaricus bisporus (abTYR), phenols and catechols are oxidized to highly reactive o-quinon

PHOTOPROXIMITY PROFILING OF PROTEIN-PROTEIN INTERACTIONS IN CELLS

Photoactive probes and probe systems for detecting biological interactions are described. The photoactive probes include probes that combine both photocleavable and photoreactive moieties. The photoactive probe systems can include a first probe comprising a photocatalytic group and a second probe comprising a group that can act as a substrate for the reaction catalyzed by the photocatalytic group. The probes and probe systems can also include groups that can specifically bind to a binding partner on a biological entity of interest and a detectable group or a precursor thereof. The probes and probe systems can detect spatiotemporal interactions of proteins or cells. In some embodiments, the interactions can be detected in live cells. Also described are methods of detecting the biological interactions.

Expanding APEX2 Substrates for Proximity-Dependent Labeling of Nucleic Acids and Proteins in Living Cells

The subcellular organization of biomolecules such as proteins and nucleic acids is intimately linked to their biological functions. APEX2, an engineered ascorbate peroxidase that enables proximity-dependent labeling of proteins in living cells, has emerged as a powerful tool for deciphering the molecular architecture of various subcellular structures. However, only phenolic compounds have thus far been employed as APEX2 substrates, and the resulting phenoxyl radicals preferentially react with electron-rich amino acid residues. This narrow scope of substrates could potentially limit the application of APEX2. In this study, we screened a panel of aromatic compounds and identified biotin-conjugated arylamines as novel probes with significantly higher reactivity towards nucleic acids. As a demonstration of the spatial specificity and depth of coverage in mammalian cells, we applied APEX2 labeling with biotin-aniline (Btn-An) in the mitochondrial matrix, capturing all 13 mitochondrial messenger RNAs and none of the cytoplasmic RNAs. APEX2-mediated Btn-An labeling of RNA is thus a promising method for mapping the subcellular transcriptome, which could shed light on its functions in cell physiology.