Maleimides are among the most frequently used reagents for thiol modification. In most proteins, the sites of reactions are at cysteine residues that either are intrinsically present or result from reduction of cystines. Unlike iodoacetamides, maleimides do not react with histidines and methionines under physiological conditions. Tetramethylrhodamine-5-maleimide is widely used for thiol modifications of peptides and proteins.
Graceffa P and Dominguez R (2003). Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J Biol Chem 278, 34172-80; Tong Y, et al. (2001). Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J Gen Physiol 117, 103-18; Tong Y, et al. (2001). Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J Gen Physiol 117, 103-18.
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