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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Yoshitaka Kimori et al.
The Biochemical journal, 450(1), 23-35 (2012-12-06)
In the present paper, we described our attempt to characterize the rough three-dimensional features of the structural analogue of the key intermediate of myosin's cross-bridge cycle. Using quick-freeze deep-etch replica electron microscopy, we observed that actin-attached myosin during in vitro
E Pate et al.
Biochemistry, 36(40), 12155-12166 (1997-10-07)
A series of ATP analogs, in which moieties of various sizes have been added to the gamma-phosphorus of ATP, bind to the active site of myosin and to the actomyosin complex in myofibrils and in chemically skinned fibers. The affinity
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
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
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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