78485
N,N′-(1,4-Phenylene)dimaleimide
≥98.0% (HPLC)
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:
assay
≥98.0% (HPLC)
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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Other Notes
Bifunctional thiol reagent for the cross-linking of proteins; Efficient procedure for the conjugation of an antibody with an enzyme
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S Yoshitake et al.
Scandinavian journal of immunology, 10(1), 81-86 (1979-01-01)
An efficient procedure for the conjugation of rabbit Fab' with beta-D-galactosidase from Escherichia coli using N,N-o-phenylenedimaleimide is described. Thiol groups of Fab' were stabilized by the presence of ethylenediaminetetraacetate, and malemide groups were shown to be stable at pH 5
P Knight
The Biochemical journal, 179(1), 191-197 (1979-04-01)
To understand the extent of the cross-linking of proteins by the bifunctional reagent p-NN'-phenylenebismaleimide, a quantitative study of competing reactions has been undertaken. The two reactive maleimide rings of the bismaleimide are hydrolysed in mildly alkaline aqueous solutions much more
J A Wells et al.
Proceedings of the National Academy of Sciences of the United States of America, 76(10), 4966-4970 (1979-10-01)
Studies with reagents that crosslink two thiol groups have shown that it is possible to trap nucleotides at the active site of myosin chymotryptic subfragment 1. Subfragment 1 incorporates nearly stoichiometric quantities of [14C]ATP or [14C]ADP in a manner that
P Knight et al.
Biochemistry, 19(20), 4682-4687 (1980-09-30)
The hypothesis that the subunits of F-actin rotate during interactin with myosin and ATP has been tested by using the specific cross-linking reagent p-phenylene-N,N'-bis(maleimide) (PM). The insertion of cross-links between F-actin subunits does not change the ability of the F-actin
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