U5378

Urea

Name: Urea
Brand: SIGMA

powder, BioReagent, Molecular Biology, suitable for cell culture

Synonym(s):

Carbamide, Carbonyldiamide

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About This Item

Linear Formula:

NH₂CONH₂

CAS Number:

57-13-6

Molecular Weight:

60.06

UNSPSC Code:

12352111

NACRES:

NA.31

PubChem Substance ID:

24900656

EC Number:

200-315-5

Beilstein/REAXYS Number:

635724

MDL number:

MFCD00008022

grade:

Molecular Biology

assay:

≥98%

technique(s):

cell culture | mammalian: suitable

Product Name

Urea, powder, BioReagent, Molecular Biology, suitable for cell culture

InChI key

XSQUKJJJFZCRTK-UHFFFAOYSA-N

InChI

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

SMILES string

NC(N)=O

grade

Molecular Biology

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

Quality Level

200

Gene Information

human ... CA1(759), CA2(760)
rat ... Ppm1a(24666)

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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.

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Labeling and identification of direct kinase substrates.

Carlson SM and White FM

Science Signaling, 5, pl3-pl3 (2012)

Construction and transfection of a ribozyme targeting human caspase-3.

Cronin D et al.

Anticancer Research, 24, 425-425 (2004)

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)

Histone acetyltransferase MoHat1 acetylates autophagy-related proteins MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and pathogenicity in Magnaporthe oryzae.

Ziyi Yin et al.

Autophagy, 15(7), 1234-1257 (2019-02-20)

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

The 3' addition of CCA to mitochondrial tRNASer(AGY) is specifically impaired in patients with mutations in the tRNA nucleotidyl transferase TRNT1.

Florin Sasarman et al.

Human molecular genetics, 24(10), 2841-2847 (2015-02-06)

Addition of the trinucleotide cytosine/cytosine/adenine (CCA) to the 3' end of transfer RNAs (tRNAs) is essential for translation and is catalyzed by the enzyme TRNT1 (tRNA nucleotidyl transferase), which functions in both the cytoplasm and mitochondria. Exome sequencing revealed TRNT1

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