Recombinant RIDA protein (His tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Recombinant human 2-iminobutanoate/2-iminopropanoate deaminase (RIDA) fragment (aa 2-137) is a high-purity protein product ideal for enzymatic and structural studies. This 14.5 kDa fragment maintains key functional domains and exhibits excellent solubility and stability, making it suitable for investigating reactive intermediate metabolism and RNA regulation mechanisms.

The full-length RIDA protein (UniProt P52758) is a multifunctional enzyme that catalyzes the hydrolytic deamination of enamine/imine intermediates formed during normal metabolism, facilitating ammonia release from potentially toxic metabolites. It acts on intermediates generated by pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase. Additionally, RIDA promotes endoribonucleolytic cleavage of specific transcripts by bridging YTHDF2 and the ribonuclease P/MRP complex, particularly targeting N6-methyladenosine (m6A)-containing mRNAs with a 5'-GGUUC-3' motif. The protein localizes primarily to the cytoplasm but is also found in the nucleus, peroxisomes, and mitochondria, with nuclear presence more prominent in less differentiated cells.