4-Chloro-7-nitrobenzofurazan (NBD-chloride) is a fluorescence assay reagent used to label free sulfhydryls and N-terminals within proteins. NBD-chloride is used as an enzyme inhibitor and as a trapping agent for cysteine sulfenic acid.
C165S AhpC in its sulfenate (Cys-SO-) and presumed thiolate (Cys-S-) forms at pH 7 (pKa for sulfenic acid about pH 6.1) exhibit low extinction absorbance bands around 367 and 324 nm, respectively. Sulfenic acid content of the protein can be
A fluorogenic derivatization method was developed to distinguish the protein N-terminal acetylation status. The unacetylated protein selectively reacted with 4-chloro-7-nitrobenzofurazan (NBD-Cl) at neutral pH to provide high fluorescence. In contrast, the protein with N-terminal acetylation was essentially nonfluorescent under the
Sodium-dependent glucose cotransporters (SGLT1 and SGLT2), which have a key role in the absorption of glucose in the kidney and/or gastrointestinal tract, have been proposed as a novel therapeutic strategy for diabetes and cardiomyopathy. Here we developed a simple cell-based
Parallel dip-pen nanolithography using spore- and colloid-terminated cantilevers.
Marcus A Kramer et al.
Small (Weinheim an der Bergstrasse, Germany), 8(24), 3791-3794 (2012-08-18)
Biochimica et biophysica acta, 1413(3), 159-171 (1999-11-11)
Pyridine nucleotide transhydrogenases of bacterial cytosolic membranes and mitochondrial inner membranes are proton pumps in which hydride transfer between NADP(+) and NAD(+) is coupled to proton translocation across cytosolic or mitochondrial membranes. The pyridine nucleotide transhydrogenase of Escherichia coli is
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