1187176-56-2

Usage

Chemical Properties

Light Brown Solid

Uses

Precursor to chelating agents.

Upstream product

• 162148-48-3 (7-tert-butoxycarbonylmethyl-1,4,7,10-tetraaza-cyclododec-1-yl)-acetic acid tert-butyl ester 
• 31640-94-5 2-(chloromethyl)pyridine N-oxide 
• 187240-78-4 dibenzyl 4,10-bis(2-(tert-butoxy)-2-oxoethyl)-1,4,7,10-tetraazacyclododecane-1,7-dicarboxylate 
• 294-90-6 1,4,7,10-tetraazacyclododecan 
• 162148-45-0 1,4,7,10-tetraaza-cyclododecane-1,7-dicarboxylic acid dibenzyl ester 

Downstream Products

• 947326-26-3 1,4,7,10-tetraazacyclododecane-1,7-[di(N-oxido-pyridine-2-yl)methyl]-4,10-bis(2-(acetylamino)ethylmethanesulfonothioate) 

Relevant academic research and scientific papers

A bis(pyridine N-oxide) analogue of DOTA: Relaxometric properties of the GdIII complex and efficient sensitization of visible and NIR-emitting lanthanide(III) cations including PrIIIand HoIII

We report the synthesis of a cyclen-based ligand (4,10-bis[(1-oxidopyridin-2-yl)methyl]-1,4,7,10-tetraazacyclo-dodecane-1,7-diacetic acid = L1) containing two acetate and two 2-methylpyridine N-oxide arms anchored on the nitrogen atoms of the cyclen platf

COMPOUNDS FOR SEPARATION OF RARE EARTH ELEMENTS AND S-, P-, D- METALS, METHOD OF SEPARATION, AND USE THEREOF

The present invention relates to compounds of general formula (I) for chromatographic separation of rare earth elements and/or s-, p-, d- metals, as well as to the method of the separation of rare earth elements.

Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment

Immobilized lanthanide ions offer the opportunity to refine structures of proteins and the complexes they form by using restraints obtained from paramagnetic NMR experiments. We report the design, synthesis, and spectroscopic evaluation of the lanthanide chelator, Caged Lanthanide NMR Probe 5 (CLaNP-5) readily attachable to a protein surface via two cysteine residues. The probe causes tunable pseudocontact shifts, alignment, paramagnetic relaxation enhancement, and luminescence, by chelating it to the appropriate lanthanide ion. The observation of single shifts and the finding that the magnetic susceptibility tensors obtained from shifts and alignment analyses are highly similar strongly indicate that the probe is rigid with respect to the protein backbone. By placing the probe at various positions on a model protein it is demonstrated that the size and orientation of the magnetic susceptibility tensor of the probe are independent of the local protein environment. Consequently, the effects of the probe are readily predictable using a protein structure only. These findings designate CLaNP-5 as a protein probe to deliver unambiguous high quality structural restraints in studies on protein-protein and protein-ligand interactions.