Thermo Scientific™ Coppia di sacchetti crosslinker per spettrometria di massa Pierce™ BS3-d0 e BS3-d4

A new strategy to study protein structure and function is rapidly emerging that integrates the proven utility of crosslinking with the power of mass spectrometry (MS) to yield insights into protein tertiary structure and protein complex formation. The reagents introduced here will generate MS patterns in which the resultant crosslinked peptides will differ by 4 mass units after enzymatic digestion of the crosslinked protein or protein complex.

Highlights:

• Well-characterized, high-purity, deuterium-labeled crosslinker and its hydrogen-containing analog
• Instructions edited by an expert in the crosslinking/MS strategy field
• Suberate- and glutarate-based reagent pair - provides a “molecular ruler” option to study inter- and intra-molecular distances to gain structural information not possible with just one reagent
• Efficient and convenient - requires only microgram amounts of protein; an excellent alternative to NMR or X-ray crystallography-based methods that require large amounts of protein, special solvents or crystal formation
• Reactive groups: Sulfo-NHS ester (homobifunctional)
• Reactive toward: amino groups

Note:

References Illustrating Applications of Heavy/Light Crosslinking Reagents and Mass Spectrometry Sinz, A. (2003). Chemical crosslinking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes.J. Mass Spectrom.38, 1225-1237. Dihazi, G.H. and Sinz, A. (2003). Mapping low-resolution three-dimensional protein structure using chemical crosslinking and Fourier transform ion-cyclotron resonance mass spectrometry. Rapid Commun. Mass Spectrom.17, 2005-2014. Kalkhof, S.et al.(2005).