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
Empirical Formula (Hill Notation):
C14H8N2O4
CAS Number:
Molecular Weight:
268.22
Beilstein/REAXYS Number:
249631
EC Number:
MDL number:
UNSPSC Code:
12162002
PubChem Substance ID:
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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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
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]
Agnieszka Galińska-Rakoczy et al.
Journal of molecular biology, 387(4), 869-882 (2009-04-03)
The mechanism of salt-induced actin polymerization involves the energetically unfavorable nucleation step, followed by filament elongation by the addition of monomers. The use of a bifunctional cross-linker, N,N'-(1,4-phenylene)dimaleimide, revealed rapid formation of the so-called lower dimers (LD) in which actin
L K Nitao et al.
Biochemistry, 37(47), 16704-16710 (1998-12-08)
Previous biochemical studies have shown that the SH1 (Cys707) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using reagents of different cross-linking lengths. In the presence of nucleotide, this cross-linking is accelerated. In
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