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Key Documents

P23989

Sigma-Aldrich

N,N′-(1,4-Phenylene)dimaleimide

97%

Synonym(s):

1,4-Dimaleimidobenzene, N,N′-(p-Phenylene)dimaleimide

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About This Item

Empirical Formula (Hill Notation):
C14H8N2O4
CAS Number:
Molecular Weight:
268.22
Beilstein:
249631
EC Number:
MDL number:
UNSPSC Code:
12162002
PubChem Substance ID:

Assay

97%

form

powder

mp

>300 °C (lit.)

SMILES string

O=C1C=CC(=O)N1c2ccc(cc2)N3C(=O)C=CC3=O

InChI

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

InChI key

AQGZJQNZNONGKY-UHFFFAOYSA-N

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Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Acute Tox. 4 Oral

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Ryan N Mello et al.
Biophysical journal, 102(5), 1088-1096 (2012-03-13)
We have used thiol cross-linking and electron paramagnetic resonance (EPR) to resolve structural transitions of myosin's light chain domain (LCD) and catalytic domain (CD) that are associated with force generation. Spin labels were incorporated into the LCD of muscle fibers
K Polosukhina et al.
Biochemistry, 36(39), 11952-11958 (1997-10-08)
Rate constants for the reactions of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimide (pPDM) and its monofunctional analog phenylmaleimide (PM) were measured for S1 and S1 bound to nucleotides and/or actin. The [pPDM] and [PM]
M O Steinmetz et al.
The Journal of cell biology, 138(3), 559-574 (1997-08-11)
The effect of the type of metal ion (i.e., Ca2+, Mg2+, or none) bound to the high-affinity divalent cation binding site (HAS) of actin on filament assembly, structure, and dynamics was investigated in the absence and presence of the mushroom
Yu S Borovikov et al.
Biophysical journal, 86(5), 3020-3029 (2004-04-28)
Fluorescence polarization measurements were used to study changes in the orientation and order of different sites on actin monomers within muscle thin filaments during weak or strong binding states with myosin subfragment-1. Ghost muscle fibers were supplemented with actin monomers
Q Wang et al.
Journal of molecular biology, 291(3), 683-692 (1999-08-17)
The lactose permease of Escherichia coli was expressed in two fragments (split permease), each with a Cys residue, and cross-linking was studied. Split permease with a discontinuity in either loop II/III (N2C10permease) or loop VI/VII (N6C6permease) was used. Proximity of

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