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Urea CAS#57-13-6
Strong Hydrogen-Bonding Capability: Urea forms an extensive and stable hydrogen-bond network both in the solid state and in aqueous systems, enhancing its interaction with other molecules.
Excellent Water Solubility: Due to its strong affinity for hydrogen bonding with water, urea dissolves readily, enabling efficient use in aqueous formulations and processing systems.
Chemically Stable and Reactive Structure: The sp²-hybridized carbon and partial double-bond character of the C–N bonds provide structural stability while maintaining useful chemical reactivity.
High Functional Polarity: The relatively basic carbonyl oxygen enhances urea’s molecular polarity, improving compatibility and performance in chemical, agricultural, and industrial applications.
Product Description
Product Description of Urea CAS#57-13-6
Urea displays state-dependent molecular geometry, adopting a planar configuration in the crystalline state but pyramidal nitrogen geometry in the gas-phase minimum-energy structure. In the solid phase, oxygen atoms form two N–H···O hydrogen bonds each, creating a stable hydrogen-bonding network that disrupts ideal packing and produces an open structure with ribbon-like arrangements and square cross-sectional channels. The sp²-hybridized central carbon imparts significant double-bond character to the C–N bonds, while the carbonyl oxygen shows greater basicity than in formaldehyde. Urea's high aqueous solubility arises from its strong hydrogen-bonding ability with water.
Product Application of Urea CAS#57-13-6
Urea is the primary nitrogen excretion product in mammals, synthesized in the liver from protein metabolism and eliminated in urine. It also occurs naturally in skin as an emollient with diuretic properties. In biochemistry, urea is widely used to denature proteins and solubilize insoluble protein species. It is particularly effective for renaturing proteins denatured with 6 M guanidine chloride, including inclusion bodies, and is often used in combination with guanidine hydrochloride and dithiothreitol to refold denatured proteins into their native conformations.
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