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MilliporeSigma

455598

O-Methylisourea hemisulfate salt

99%

Synonym(s):

OMI®

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100 G

$248.00

$248.00


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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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1 of 4

This Item
M53701O1376HPA050306
assay

99%

assay

99%

assay

≥99% (HPLC)

assay

-

Quality Level

200

Quality Level

100

Quality Level

200

Quality Level

100

solubility

water: soluble 100 mg/mL, clear, colorless

solubility

-

solubility

-

solubility

-

mp

163-167 °C (lit.)

mp

118-120 °C (lit.)

mp

-

mp

-

form

solid

form

-

form

powder

form

buffered aqueous glycerol solution

functional group

amine

functional group

-

functional group

-

functional group

-

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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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
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)
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
Optimization of guanidination procedures for MALDI mass mapping.
Beardsley RL and Reilly JP.
Analytical Chemistry, 74(8), 1884-1890 (2002)

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