948039-60-9

Upstream product

• 3695-77-0 triphenylmethanethiol 
• 178685-33-1 8-azido-3,6-dioxaoctyl tosylate 
• 112-27-6 2,2'-[1,2-ethanediylbis(oxy)]bisethanol 
• 86927-04-0 2-(2-(2-(2-bromoethoxy)ethoxy)ethyl)-isoindole-1,3(2H)-dione 
• 31255-10-4 1,2-bis-(2-bromo-ethoxy)-ethane 
• 948039-05-2 S-2-(2-(2-phthalimidoethoxy)ethyl) ethanethiolate 
• 948039-59-6 2-(2-(2-aminoethoxy)ethoxy)ethanethiol 
• 76-83-5 trityl chloride 

Downstream Products

• 948039-69-8 4-sulfamoyl-N-{2-[2-(2-tritylsulfanyl-ethoxy)-ethoxy]-ethyl}-benzamide 
• 1429636-94-1 C₂₂H₃₅N₇O₈S*C₂HF₃O₂ 

Relevant academic research and scientific papers

The first ready-to-use benzene-based heterotrifunctional cross-linker for multiple bioconjugation

The synthesis and applications of the first water-soluble benzene derivative bearing a set of three different and orthogonal bioconjugatable groups (aminooxy, azido and thiol) are described. The combined use of a 5-amino isophthalic acid scaffold and unusual acid-labile protecting groups for temporarily masking aminooxy and thiol moieties has enabled the development of a highly convergent approach towards the synthesis of such a trivalent bioconjugation platform in good yields. The potential utility of this ready-to-use cross-linking reagent for creating complex and fragile tri-component (bio)molecular systems was illustrated through (1) the rapid preparation of a three-colour FRET cascade with valuable spectral properties and (2) the luminescent/fluorescent labelling of peptides and peptide- oligonucleotide conjugates. Thus, such (bio)molecular assemblies were readily obtained via a three-step process or in a one-pot manner, both involving oxime ligation, thiol-alkylation (SN2 or Michael addition) and copper-catalysed azide-alkyne 1,3-dipolar cycloaddition (CuAAC) reactions.

Label-free detection of protein-protein interactions on biochips

(Figure Presented) Eliminating the middle-man: The combination of MALDI-TOF mass spectrometry and self-assembled monolayers on gold (SAMDI) offers a new detection method for protein-ligand (shown) and protein-protein interactions. Proteins and protein complexes are selectively bound to biochips and then directly analyzed by MALDI-TOF MS without the need for labels.