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104590

Sigma-Aldrich

N,N′-(o-Phenylene)dimaleimide

99%

Sinónimos:

1,2-Dimaleimidobenzene

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About This Item

Fórmula empírica (notación de Hill):
C14H8N2O4
Número de CAS:
13118-04-2
Peso molecular:
268.22
Beilstein/REAXYS Number:
249426
EC Number:
236-046-5
MDL number:
MFCD00005503
UNSPSC Code:
12162002
PubChem Substance ID:
24846652
NACRES:
NA.23

assay

99%

mp

245-247 °C (dec.) (lit.)

SMILES string

O=C1C=CC(=O)N1c2ccccc2N3C(=O)C=CC3=O

InChI

1S/C14H8N2O4/c17-11-5-6-12(18)15(11)9-3-1-2-4-10(9)16-13(19)7-8-14(16)20/h1-8H

InChI key

UFFVWIGGYXLXPC-UHFFFAOYSA-N

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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T Katoh et al.
European journal of biochemistry, 227(1-2), 459-465 (1995-01-15)
Porcine aorta myosin was reacted with a bifunctional cross-linking reagent, N,N'-o-phenylenedimaleimide. The 17-kDa essential light chain (LC17) in each myosin head was intramolecularly cross-linked within a single myosin molecule. The 34-kDa cross-linked LC17 dimer was isolated and its peptide map
M Elzinga et al.
Proceedings of the National Academy of Sciences of the United States of America, 81(21), 6599-6602 (1984-11-01)
The bifunctional reagent N,N'-p-phenylenedimaleimide (PDM) is being used in an attempt to measure distances between specific side chains in adjacent monomers within F-actin. [14C]PDM was synthesized and was used to crosslink F-actin. Uncrosslinked actin was removed by gel filtration, and
L E Greene et al.
Biochemistry, 25(3), 704-709 (1986-02-11)
In our previous study [Chalovich, J. M., Greene, L. E., & Eisenberg, E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 4909-4913], myosin subfragment 1 that was modified by having its two reactive thiol groups cross-linked by N,N'-p-phenylenedimaleimide (pPDM) was found
R T King et al.
The Journal of biological chemistry, 262(13), 6128-6134 (1987-05-05)
Electron microscopy studies have shown that the structure of the complex of myosin subfragment 1 (S-1) cross-linked to actin with 1-ethyl-3-[3-(dimethyl-amino) propyl] carbodiimide is very different in the presence and absence of ATP (Craig, R., Greene, L. E., and Eisenberg
D Applegate et al.
The Journal of biological chemistry, 262(14), 6856-6863 (1987-05-15)
Unstained frozen hydrated samples of myosin subfragment 1 (S-1) cross-linked to actin with the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide have been examined by electron microscopy in an effort to probe structural states of the attached cross-bridge. The cross-linked complex in the absence
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