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P23989

N,N′-(1,4-Phenylene)dimaleimide

Name: <I>N,N′</I>-(1,4-Phenylene)dimaleimide
Brand: ALDRICH

97%

Sinonimo/i:

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

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About This Item

Formula empirica (notazione di Hill):

C₁₄H₈N₂O₄

Numero CAS:

3278-31-7

Peso molecolare:

268.22

Beilstein:

249631

Numero CE:

221-910-6

Numero MDL:

MFCD00005505

Codice UNSPSC:

12162002

ID PubChem:

24898322

Prodotti consigliati

Slide 1 of 1

1 of 1

Sigma-Aldrich

ZRB1430

Anti-MCL-1 Antibody, clone 2O7 ZooMAb^® Rabbit Monoclonal

Saggio

97%

Forma fisica

powder

Punto di fusione

>300 °C (lit.)

Stringa SMILE

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
AQGZJQNZNONGKY-UHFFFAOYSA-N

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Pittogrammi

GHS07

Avvertenze

Warning

Indicazioni di pericolo

H302

Classi di pericolo

Acute Tox. 4 Oral

Codice della classe di stoccaggio

13 - Non Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

dust mask type N95 (US), Eyeshields, Gloves

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Three distinct actin-attached structural states of myosin in muscle fibers.

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

Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities.

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]

A correlative analysis of actin filament assembly, structure, and dynamics.

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

Fluorescence depolarization of actin filaments in reconstructed myofibers: the effect of S1 or pPDM-S1 on movements of distinct areas of actin.

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

Proximity relationships between helices I and XI or XII in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking.

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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