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Key Documents

455598

Sigma-Aldrich

O-Methylisourea hemisulfate salt

99%

Synonym(s):

OMI®

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About This Item

Linear Formula:
H2NC(OCH3)=NH · 1/2H2SO4
CAS Number:
Molecular Weight:
123.12
Beilstein:
3723107
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22

Quality Level

Assay

99%

form

solid

mp

163-167 °C (lit.)

solubility

water: soluble 100 mg/mL, clear, colorless

functional group

amine

SMILES string

COC(N)=N.COC(N)=N.OS(O)(=O)=O

InChI

1S/2C2H6N2O.H2O4S/c2*1-5-2(3)4;1-5(2,3)4/h2*1H3,(H3,3,4);(H2,1,2,3,4)

InChI key

QSCPQKVWSNUJLJ-UHFFFAOYSA-N

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Legal Information

OMI is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Optimization of guanidination procedures for MALDI mass mapping.
Beardsley RL and Reilly JP.
Analytical Chemistry, 74(8), 1884-1890 (2002)
Valerie J Carabetta et al.
Journal of the American Society for Mass Spectrometry, 21(6), 1050-1060 (2010-03-09)
The study of isolated protein complexes has greatly benefited from recent advances in mass spectrometry instrumentation and quantitative, isotope labeling techniques. The comprehensive characterization of protein complex components and quantification of their relative abundance relies heavily upon maximizing protein and
K M Fazili et al.
Biochemistry and molecular biology international, 31(5), 807-816 (1993-12-01)
Using acetic anhydride, potassium cyanate and O-methyl isourea six chemically modified derivatives of bovine serum albumin with chemical modification on lysine side chains have been prepared. All the modified preparations were found to be homogeneous with respect to size and
Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique.
H R Wenzel et al.
FEBS letters, 140(1), 53-57 (1982-04-05)
Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1.
K Mita et al.
Biopolymers, 20(6), 1103-1112 (1981-06-01)

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