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Description
To test our previous hypothesis that, among GUS family members, L1 GUS enzymes most efficiently process small glucuronide substrates, we cloned, expressed and purified two previously uncharacterized L1 GUS enzymes, Rg GUS and Lr GUS, for subsequent structural and functional studies

These alternatives, often employed for their perceived safety, accessibility, and potential anti-inflammatory or immunomodulatory properties, represent an important area of investigation, especially in regions where traditional practices are deeply embedded within healthcare systems [21, 22]

Quantitative Accuracy: Isotope-dilution LC-MS/MS achieves 85115% recovery with relative error 15% across multiple matrices

Reverse transcription reactions (20 l) were carried out with SuperScript III reverse transcriptase (Thermo Fisher, 18080085) according to the manufacturers instructions and containing 4 l 5x first-strand buffer, 1 l of murine RNase inhibitor (NEB, 174M0314S), 1 l of 10 mM dNTP mix (Thermo Fisher, 18427-013), 50 ng of random hexamers (Bioline, BIO-38028), and 1 g of total RNA (in a total volume of 11 l)
