253375
3-Maleimido-PROXYL
free radical
Synonym(s):
3-Maleimido-2,2,5,5-tetramethyl-1-pyrrolidinyloxy, free radical
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About This Item
Empirical Formula (Hill Notation):
C12H17N2O3
CAS Number:
Molecular Weight:
237.27
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352005
MDL number:
InChI
1S/C12H17N2O3/c1-11(2)7-8(12(3,4)14(11)17)13-9(15)5-6-10(13)16/h5-6,8H,7H2,1-4H3
SMILES string
CC1(C)CC(N2C(=O)C=CC2=O)C(C)(C)N1[O]
InChI key
HGNHBHXFYUYUIA-UHFFFAOYSA-N
mp
111-113 °C (lit.)
functional group
imide, maleimide
storage temp.
2-8°C
Quality Level
Application
Spin label used for study of local protein structure and for determining molecular changes in erythrocyte membranes.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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P D Morse
Biochimica et biophysica acta, 844(3), 337-345 (1985-03-21)
In a recent paper, Daveloose et al. (Daveloose, D., Fabre, G., Berleur, F., Testylier, G. and Letterrier, F. (1983) Biochim. Biophys. Acta 763, 41-49) described a technique to measure the internal microviscosity of erythrocytes using the spin label MAL-3 (2,2,5,5-tetramethyl-3-malimidopyrrolidinyl-N-oxyl)
Oleg Y Dmitriev et al.
Biochimica et biophysica acta, 1777(2), 227-237 (2008-01-08)
Subunit a in the membrane traversing F0 sector of Escherichia coli ATP synthase is known to fold with five transmembrane helices (TMHs) with residue 218 in TMH IV packing close to residue 248 in TMH V. In this study, we
Angela Tseng et al.
Journal of food science, 77(9), H192-H201 (2012-08-23)
The effects of different drying methods (40 °C conventional and vacuum oven, 25 °C ambient air and freeze dry) on the stability of two red wine grape (Pinot Noir, PN and Merlot, M) byproducts, pomace containing skins and seeds (P)
Brett A Colson et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(12), 3233-3238 (2016-02-26)
We have used the site-directed spectroscopies of time-resolved fluorescence resonance energy transfer (TR-FRET) and double electron-electron resonance (DEER), combined with complementary molecular dynamics (MD) simulations, to resolve the structure and dynamics of cardiac myosin-binding protein C (cMyBP-C), focusing on the
L Zhao et al.
Biophysical journal, 69(3), 994-999 (1995-09-01)
Electron paramagnetic resonance spectroscopy of a spin probe attached to cys-707 on myosin cross-bridges was used to monitor the orientation of the myosin catalytic domain at the beginning and end of the working power stroke in active muscle. Elevated concentrations
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