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Merck

455598

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
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
EC Number:
257-851-8
Beilstein/REAXYS Number:
3723107
MDL number:
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Product Name

O-Methylisourea hemisulfate salt, 99%

InChI key

QSCPQKVWSNUJLJ-UHFFFAOYSA-N

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)

SMILES string

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

assay

99%

form

solid

mp

163-167 °C (lit.)

solubility

water: soluble 100 mg/mL, clear, colorless

functional group

amine

Quality Level

Gene Information

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Legal Information

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

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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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
E Guerrero et al.
Molecular immunology, 27(5), 435-441 (1990-05-01)
Lysine residue 122 of the major protein of HBsAg/adw has been shown previously to be involved in the d subtype determinant. We demonstrate here that the corresponding residue of the HBsAg/ayw, arginine 122, does not play such a critical role
H Wojciechowska et al.
Acta biochimica Polonica, 29(3-4), 197-204 (1982-01-01)
Selectivity of amidination using ornithine as model amino acid was investigated in detail. The results obtained were taken advantage of for studying the reactions with other polyfunctional amino acids: beta-tyrosine, isoserine, 2,3-diaminopropionic acid, 2,6-diamino-7-hydroxyazelaic acid and with the pentapeptide amide

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