Recombinant Human HPRT protein

**Background of HPRT Recombinant Protein**

Hypoxanthine-guanine phosphoribosyltransferase (HPRT) is a critical enzyme in the purine salvage pathway, a metabolic route that recycles purine bases to synthesize nucleotides. It catalyzes the conversion of hypoxanthine and guanine into inosine monophosphate (IMP) and guanosine monophosphate (GMP), respectively, using phosphoribosyl pyrophosphate (PRPP) as a co-substrate. HPRT deficiency in humans is linked to severe disorders, such as Lesch-Nyhan syndrome, a rare X-linked genetic disease characterized by neurological dysfunction, hyperuricemia, and self-injurious behavior.

Recombinant HPRT protein is produced using genetic engineering techniques, typically by expressing the *HPRT1* gene in bacterial, yeast, or mammalian expression systems. *E. coli* is a common host due to its cost-effectiveness and high yield, though post-translational modifications may require eukaryotic systems. The purified recombinant protein retains enzymatic activity, enabling its use in biochemical assays, drug screening, and mechanistic studies of purine metabolism.

In research, recombinant HPRT serves as a tool to study enzyme kinetics, substrate specificity, and inhibition, aiding the development of therapies for conditions like gout or cancer where purine metabolism is dysregulated. It is also employed in cell culture systems, such as HPRT-deficient cell lines, for selection purposes in genetic engineering (e.g., CRISPR or gene knockout studies). Additionally, recombinant HPRT is explored in gene therapy and enzyme replacement strategies for HPRT-related disorders.

Overall, HPRT recombinant protein bridges fundamental biochemistry with clinical applications, offering insights into metabolic diseases and therapeutic innovations. Its versatility underscores its importance in both academic and pharmaceutical contexts.