Beyond its critical role in RNA isolation, Diethyl Pyrocarbonate (DEPC) is a valuable tool in protein chemistry, specifically for targeted modifications. Its reactivity with imidazole rings makes it an effective reagent for altering histidine residues, and it also reacts with tyrosine residues. These modifications are instrumental in various biochemical studies, including understanding enzyme mechanisms, protein structure-function relationships, and developing novel probes for biological systems. As a leading chemical supplier, we provide high-purity DEPC that meets the stringent requirements for such precise biochemical manipulations.

The modification of histidine residues by DEPC is particularly significant because histidine is a common catalytic residue in many enzymes. By reacting with the imidazole nitrogen of histidine, DEPC can irreversibly inhibit enzyme activity or alter the chemical environment around the active site, providing insights into the enzyme's catalytic mechanism. Similarly, its reaction with tyrosine residues can be used to probe protein structure or to introduce functional groups for further conjugation. These applications highlight the versatility of Diethyl Pyrocarbonate as a biochemical reagent. Researchers often seek to buy DEPC for its well-established efficacy in these protein modification studies.

As a manufacturer committed to quality, we ensure that our Diethyl Pyrocarbonate (CAS 1609-47-8) is suitable for these advanced applications. The ability to selectively modify amino acid residues allows scientists to dissect protein function, map active sites, and even develop new therapeutic agents. Whether you are investigating enzyme kinetics or engineering proteins with novel properties, the precision offered by DEPC makes it an indispensable reagent. Our role as a reliable supplier in China means we can support your research endeavors with consistent access to this essential chemical. Understanding the chemical properties and reaction mechanisms of DEPC is key to maximizing its potential in protein modification experiments.