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U5378

Sigma-Aldrich

Urea

powder, BioReagent, for molecular biology, suitable for cell culture

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Synonym(s):
Carbamide, Carbonyldiamide
Linear Formula:
NH2CONH2
CAS Number:
Molecular Weight:
60.06
Beilstein:
635724
EC Number:
MDL number:
UNSPSC Code:
12352111
PubChem Substance ID:
NACRES:
NA.31

grade

for molecular biology

Quality Level

product line

BioReagent

Assay

≥98%

form

powder

technique(s)

cell culture | mammalian: suitable

mp

132-135 °C (lit.)

solubility

H2O: soluble 480 mg/mL, clear, colorless (8M)

density

1.335 g/mL at 25 °C (lit.)

anion traces

chloride (Cl-): ≤5 ppm

cation traces

Cu: ≤1 ppm
Fe: ≤5 ppm
Pb: ≤2 ppm

absorption

≤0.06 at 260 at 6 M
≤0.06 at 280 at 6 M

foreign activity

DNase, NICKase, RNase and protease, none detected

SMILES string

NC(N)=O

InChI

1S/CH4N2O/c2-1(3)4/h(H4,2,3,4)

InChI key

XSQUKJJJFZCRTK-UHFFFAOYSA-N

Gene Information

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Application

  • Urea has been used in protein resuspension buffer and to denature proteins.
  • It has been used for the isolation of proteins via urea-containing polyacrylamide gels.
  • It has been used to study the conformation of unfolded proteins under different concentrations of urea and different pH.
Used for the denaturation of proteins and as a mild solubilization agent for insoluble or denatured proteins. Useful for renaturing proteins from samples already denatured with 6 M guanidine chloride such as inclusion bodies. May be used with guanidine hydrochloride and dithiothreitrol (DTT) in the refolding of denatured proteins into their native or active form.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Construction and transfection of a ribozyme targeting human caspase-3.
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Structure and properties of native and unfolded lysing enzyme from T. harzianum: Chemical and pH denaturation.
Bey H et al.
International Journal of Biological Macromolecules, 92, 860-860 (2016)
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Macroautophagy/autophagy is critical for normal appressorium formation and pathogenicity of the rice blast fungus Magnaporthe oryzae, but the molecular base of autophagy linked to pathogenicity remains elusive in this or other pathogenic fungi. We found that MoHat1, a histone acetyltransferase
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