Date published: 2025-12-18

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RNase Inhibitors

Santa Cruz Biotechnology now offers a broad range of RNase Inhibitors for use in various applications. RNase Inhibitors are a critical category of enzymes used extensively in molecular biology and biochemical research. They function by inhibiting ribonucleases (RNases), enzymes that degrade RNA molecules. This inhibition is essential in experiments where RNA integrity is paramount, such as RNA sequencing, cDNA synthesis, and RNA protection assays. By preventing RNase activity, RNase Inhibitors help maintain the stability and purity of RNA samples, allowing for accurate and reliable analysis. These inhibitors are particularly valuable in labs focused on gene expression studies, RNA-based research, and the development of RNA technologies. RNase Inhibitors have become a cornerstone in the toolkit of molecular biologists, enabling them to explore RNA-related processes without the degradation that would otherwise complicate or invalidate results. Santa Cruz Biotechnology's RNase Inhibitors are available in various formulations and concentrations, catering to different research needs and experimental conditions. View detailed information on our available RNase Inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Guanidine Hydrochloride

50-01-1sc-202637
sc-202637A
100 g
1 kg
$60.00
$195.00
1
(2)

Guanidine Hydrochloride is a potent denaturant that disrupts hydrogen bonding and hydrophobic interactions within nucleic acids and proteins. Its high solubility in water enhances its ability to unfold RNA structures, facilitating the exposure of active sites. This disruption can significantly alter reaction kinetics, promoting the degradation of RNA by RNases. The compound's ionic nature also influences electrostatic interactions, further modulating enzymatic activity and stability.

Rugulosin (+ form)

23537-16-8sc-202327
1 mg
$281.00
1
(1)

Rugulosin exhibits unique properties as an RNase, characterized by its ability to selectively bind to RNA substrates through specific hydrogen bonding and hydrophobic interactions. This binding enhances the enzyme's catalytic efficiency, facilitating the cleavage of phosphodiester bonds. The compound's structural conformation allows for optimal alignment with RNA, influencing reaction kinetics and promoting rapid degradation. Additionally, its interactions with metal ions can modulate enzymatic activity, further impacting RNA stability.