IMPDH1 is a ubiquitous enzyme found in both the cytosol and nucleus of cells. It plays a central role in the regulation of cell growth and differentiation by controlling the intracellular levels of guanine nucleotides . The enzyme is composed of 534 amino acids and has a molecular mass of approximately 57.5 kDa . The recombinant form of IMPDH1 is often produced in E. coli and is purified using proprietary chromatographic techniques .
IMPDH1 is a target for various immunosuppressive drugs, antiviral agents, and cancer therapeutics. Inhibitors of IMPDH1 are used to suppress the immune system in organ transplantation and to treat certain viral infections and cancers . The recombinant form of IMPDH1 is used in research to study its structure, function, and interactions with potential inhibitors.
Recombinant IMPDH1 is typically produced using baculovirus expression systems in insect cells or bacterial expression systems in E. coli . The protein is then purified through a series of chromatographic steps to achieve high purity and activity. The recombinant protein is often tagged with a His-tag to facilitate purification and detection .
The activity of recombinant IMPDH1 can be measured by its ability to convert IMP to XMP in the presence of NAD . The specific activity of the enzyme is determined under defined conditions, and the reaction can be monitored using spectrophotometric assays . The enzyme’s activity is crucial for maintaining the balance of guanine nucleotides in cells, and its inhibition can lead to reduced cell proliferation and immune response .
IMPDH1 continues to be a significant focus of research due to its essential role in nucleotide metabolism and its potential as a therapeutic target.