GDA Human, Active
Description
GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Recombinant human guanine deaminase is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein often includes a His-tag at the N-terminus to facilitate purification through affinity chromatography . The enzyme consists of 454 amino acids and has a molecular weight of approximately 53 kDa . The His-tagged version of the protein allows for easy identification and isolation during experimental procedures.
Guanine deaminase is responsible for the deamination of guanine to xanthine, a reaction that is part of the purine degradation pathway. This pathway is crucial for maintaining the balance of purine nucleotides within the cell. The specific activity of recombinant human guanine deaminase is typically greater than 2,000 pmol/min/μg, which is defined as the amount of enzyme that converts guanine to xanthine per minute at pH 8.0 and 37°C .
The enzyme’s activity is not only important for nucleotide metabolism but also has implications in various physiological processes. Studies in rat orthologs suggest that guanine deaminase may play a role in microtubule assembly . This indicates potential involvement in cellular processes such as cell division and intracellular transport.
Recombinant human guanine deaminase is widely used in biochemical and physiological research. Its high purity and specific activity make it suitable for various applications, including enzyme kinetics studies, structural biology, and drug discovery. The enzyme’s role in purine metabolism also makes it a target for research into metabolic disorders and potential therapeutic interventions.
For optimal stability, recombinant human guanine deaminase should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the enzyme’s activity .
In summary, guanine deaminase is a vital enzyme in purine metabolism with significant roles in cellular processes. The recombinant form, produced in E. coli, provides a valuable tool for scientific research, offering insights into enzyme function and potential therapeutic applications.
