P23989
N,N′-(1,4-Phenylene)dimaleimide
97%
Synonym(s):
1,4-Dimaleimidobenzene, N,N′-(p-Phenylene)dimaleimide
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About This Item
Recommended Products
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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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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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
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]
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
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
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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