Description
  • What it is. This urea is supplied as ACS reagent-grade white crystals in a 1 lb size. This high-purity organic compound is used as a protein denaturant, nitrogen source, and reagent in biochemistry, analytical chemistry, and teaching labs.
  • What ACS grade guarantees. ACS reagent urea assays at 99.0 to 100.5%, melts at 132 to 135 °C, and limits insoluble matter and sulfated ash to 0.01% each, iron and heavy metals to 0.001% each, chloride to 5 ppm, and sulfate to 0.001%.
  • Chemical identity. Urea (carbamide, CAS 57-13-6, CH4N2O, 60.06 g/mol) is the diamide of carbonic acid. It is highly soluble in water and was the first organic compound synthesized from inorganic starting materials in 1828.
  • Protein denaturant. Concentrated urea solutions, typically 6-8 M, unfold proteins by disrupting hydrogen bonds and hydrophobic interactions. Urea solubilizes inclusion bodies, denatures proteins for electrophoresis, and supports protein refolding studies.
  • Nucleic acid work. Urea is a component of denaturing polyacrylamide gels for DNA and RNA electrophoresis, where it keeps nucleic acids single-stranded so they separate by length.
  • Use fresh solutions. Urea in solution slowly decomposes to ammonium cyanate, which can carbamylate proteins and alter their charge. Prepare urea solutions fresh, avoid heating them, and deionize stored solutions if you must keep them.
  • Other uses. Urea serves as a nitrogen standard and reagent in analytical chemistry, in fertilizer and feed research, as a moisturizer in cosmetics, in diesel exhaust fluid for emission control, and in teaching labs.
  • Preparing urea solutions. Dissolving urea absorbs heat, so solutions cool noticeably as it dissolves. Allow them to return to room temperature before adjusting volume. Use high-purity water, and filter solutions for electrophoresis or chromatography.
  • Handling at a glance. Urea is low hazard, but dust may irritate the eyes and respiratory tract. Wear safety glasses and gloves, avoid creating dust, and keep the container tightly closed since urea absorbs moisture.

Technical Specifications

Chemical Name Urea
CAS Number 57-13-6
EC Number 200-315-5
Synonyms Carbamide, carbonyl diamide
Formula CH4N2O (NH2CONH2)
Molecular Weight 60.06 g/mol
Grade ACS reagent
Assay 99.0 to 100.5%
Melting Range 132 to 135 °C
Insoluble Matter 0.01% max
Sulfated Ash / Residue after Ignition 0.01% max
Chloride (Cl) 5 ppm max
Sulfate (SO4) 0.001% max
Iron (Fe) 0.001% max
Heavy Metals (as Pb) 0.001% max
Form White crystals
Water Solubility Highly soluble
Typical Denaturing Concentration 6 to 8 M
Hazard Profile Not classified as hazardous (confirm on SDS)
Package Size 1 lb

Applications / Common Uses

  • Protein denaturation: Unfolds proteins at 6 to 8 M.
  • Denaturing gels: Keeps DNA and RNA single-stranded.
  • Inclusion body solubilization: Dissolves aggregated recombinant proteins.
  • Analytical reagent: Serves as a nitrogen standard and reagent.
  • Teaching labs: Demonstrates organic synthesis history and protein chemistry.

Storage, Handling & Shipping

Store tightly closed in a cool, dry place at room temperature, away from strong oxidizers, nitrites, and hypochlorites. Urea absorbs moisture, so reseal the container promptly and prepare solutions fresh rather than storing them long term.

  • Incompatible materials: Strong oxidizers, sodium hypochlorite, nitrites, and strong acids.
  • Personal protection: Safety glasses, gloves, and dust control.
  • Spill response: Sweep up without raising dust and place in a closed container.
  • First aid: Eyes: rinse with water for several minutes.

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FAQs

What is ACS grade urea used for?

It denatures proteins, solubilizes inclusion bodies, prepares denaturing polyacrylamide gels for DNA and RNA, serves as a nitrogen standard and analytical reagent, and supports teaching labs. ACS grade limits impurities such as metals, chloride, and sulfate that could affect sensitive work. It is a staple biochemistry reagent.

How does urea denature proteins?

At concentrations around 6 to 8 M, urea disrupts the hydrogen bonds and hydrophobic interactions that hold proteins in their folded shape. The protein unfolds into a flexible chain, which helps solubilize aggregates and allows studies of folding and refolding. Removing urea by dialysis allows refolding studies.

Why should urea solutions be made fresh?

Urea in water slowly converts to ammonium cyanate. Cyanate reacts with protein amino groups (carbamylation), changing protein charge and potentially interfering with analysis. Prepare solutions fresh, avoid heating them, and deionize any solution that must be stored. Mixed-bed resin removes cyanate.

How much urea makes an 8 M solution?

Dissolve about 480.5 g of urea in water and bring the volume to 1 liter (calculated from 60.06 g/mol). Dissolution absorbs heat and cools the solution, so allow it to warm to room temperature before adjusting the final volume. Mix until fully dissolved and filter if needed before use.

Is urea hazardous?

Urea has low toxicity and is not generally classified as hazardous. Dust may irritate the eyes and respiratory tract, so wear safety glasses and gloves and avoid creating dust. Keep it away from hypochlorite and nitrites, as it can react with them. Store it dry. Store it dry.