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253375

3-Maleimido-PROXYL

Name: 3-Maleimido-PROXYL
Brand: ALDRICH

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:

5389-27-5

Molecular Weight:

237.27

NACRES:

NA.22

PubChem Substance ID:

24855309

UNSPSC Code:

12352005

MDL number:

MFCD00010167

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Properties

Quality Level

100

mp

111-113 °C (lit.)

functional group

imide, maleimide

storage temp.

2-8°C

SMILES string

CC1(C)CC(N2C(=O)C=CC2=O)C(C)(C)N1[O]

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

InChI key

HGNHBHXFYUYUIA-UHFFFAOYSA-N

Description

Application

Spin label used for study of local protein structure and for determining molecular changes in erythrocyte membranes.

pictograms

GHS07

signalword

Warning

hcodes

H315,H319,H335

pcodes

P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338

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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A new spin label method for the measurement of erythrocyte internal microviscosity.

D Daveloose et al.

Biochimica et biophysica acta, 763(1), 41-49 (1983-08-17)

A new spin-label method for the measurement of the internal microviscosity of erythrocyte is presented. The spin label used is 2,2',5,5'-tetramethyl-3-maleimidopyrrolidinyl-N-oxyl (MAL-5) which penetrates inside the red blood cell and binds covalently on cytoplasmic glutathione. After washing off the external

Membrane assembly of the 16-kDa proteolipid channel from Nephrops norvegicus studied by relaxation enhancements in spin-label ESR.

T Páli et al.

Biochemistry, 38(43), 14311-14319 (1999-11-26)

The 16-kDa proteolipid from the hepatopancreas of Nephrops norvegicus belongs to the class of channel proteins that includes the proton-translocation subunit of the vacuolar ATPases. The membranous 16-kDa protein from Nephrops was covalently spin-labeled on the unique cysteine Cys54, with

Site-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics.

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

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Global Trade Item Number

SKU	GTIN
253375-25MG	04061833278925