866822-65-3

Basic information

• Product Name: L-Lysine, L-tyrosyl-L-isoleucyl-L-prolylglycyl-L-threonyl-L-lysyl-L-methionyl-L-isoleucyl -L-phenylalanyl-L-alanylglycyl-L-isoleucyl-
• CAS NO: 866822-65-3
• Molecular Formula: C69H111N15O16S
• Molecular Weight: 1438.8
• Mol File: 866822-65-3.mol

Chemical Properties

• CAS DataBase Reference: L-Lysine, L-tyrosyl-L-isoleucyl-L-prolylglycyl-L-threonyl-L-lysyl-L-methionyl-L-isoleucyl -L-phenylalanyl-L-alanylglycyl-L-isoleucyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Lysine, L-tyrosyl-L-isoleucyl-L-prolylglycyl-L-threonyl-L-lysyl-L-methionyl-L-isoleucyl -L-phenylalanyl-L-alanylglycyl-L-isoleucyl-(866822-65-3)
• EPA Substance Registry System: L-Lysine, L-tyrosyl-L-isoleucyl-L-prolylglycyl-L-threonyl-L-lysyl-L-methionyl-L-isoleucyl -L-phenylalanyl-L-alanylglycyl-L-isoleucyl-(866822-65-3)

Safety Data

• Hazardous Substances Data: 866822-65-3(Hazardous Substances Data)

Relevant articles and documents

Shift reagents for multidimensional ion mobility spectrometry-mass spectrometry analysis of complex peptide mixtures: Evaluation of 18-crown-6 ether complexes

18-Crown-6 ether (18C6) is evaluated as a shift reagent for multidimensional ion mobility spectrometry-mass spectrometry (IMS-IMS-MS) analyses of tryptic protein digests. In this approach, 18C6 is spiked into the solution-phase mixture and noncovalent peptide-crown ion complexes are formed by electrospraying the mixture into the gas phase. After an initial mobility separation in the first IMS drift region, complexes of similar mobility are selected and dissociated via collisional activation prior to entering the second drift region. These dissociation products (including smaller complexes, naked peptide ions, charge transfer products, and fragment ions) differ in mobility from their precursor ion complexes and (in favorable cases) from one another, allowing the mixture to resolve further in the second IMS region. We estimate an IMS-IMS peak capacity of ～2400 when shift reagents are employed. The approach is illustrated by examining a tryptic digest of cytochrome c and by identifying a peptide out of a complex mixture obtained by digestion of human plasma proteins. Disadvantages arising from increased complexity of data sets as well as other advantages of this approach are considered.

Efficient tryptic proteolysis accelerated by laser radiation for peptide mapping in proteome analysis

Back to basics: Coupled with MALDI-TOF MS, laser-assisted proteolysis (see schematic illustration) enabled rapid protein digestion and peptide mapping without the need for enzyme immobilization to increase the efficiency of tryptic digestion. Protein solutions containing trypsin were digested in less than a minute upon irradiation at 808 nm with a laser.