InChI key
VCUVETGKTILCLC-UHFFFAOYSA-N
InChI
1S/C6H11NO/c1-6(2)4-3-5-7(6)8/h5H,3-4H2,1-2H3
SMILES string
CC1(C)CCC=[N+]1[O-]
assay
97%
refractive index
n20/D 1.496 (lit.)
bp
75 °C/0.4 mmHg (lit.)
mp
25-29 °C (lit.)
density
1.015 g/mL at 25 °C (lit.)
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Application
神经保护剂;一氧化氮自旋捕获剂。用于研究通过酶促乙醛氧化反应形成的自由基。
神经保护剂;一氧化氮自旋捕获剂。用于研究通过酶促乙醛氧化反应形成的自由基。用DMPO孵育淋巴细胞,可减少NiCl2对DNA的损伤。
Spin-trapping reagent used to study the formation of hydroxyl and superoxide radicals.
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
203.0 °F - closed cup
flash_point_c
95 °C - closed cup
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
S Pou et al.
Analytical biochemistry, 217(1), 76-83 (1994-02-15)
The spin trap 5,5-dimethyl-1-pyrroline-1-oxide (DMPO) alone, as well as DMPO or N-tert-butyl-alpha-phenylnitrone (PBN) in the presence of excess dimethyl sulfoxide (Me2SO), have been used as spin trapping systems for the detection of hydroxyl radical. However, the instability of DMPO and
Free Radical Res. Commun., 17, 377-377 (1992)
Xiaoguang Duan et al.
Small (Weinheim an der Bergstrasse, Germany), 11(25), 3036-3044 (2015-03-20)
Sulfur and nitrogen co-doped reduced graphene oxide (rGO) is synthesized by a facile method and demonstrated remarkably enhanced activities in metal-free activation of peroxymonosulfate (PMS) for catalytic oxidation of phenol. Based on first-order kinetic model, S-N co-doped rGO (SNG) presents
Sambuddha Banerjee et al.
Free radical biology & medicine, 53(6), 1317-1326 (2012-07-31)
We compared oxygenation and anaerobic oxidation reactions of a purified complex of human hemoglobin (Hb) and haptoglobin (Hb-Hp) to those of uncomplexed Hb. Under equilibrium conditions, Hb-Hp exhibited active-site heterogeneity and noncooperative, high-affinity O(2) binding (n(1/2)=0.88, P(1/2)=0.33 mm Hg in
Patrick T Kang et al.
Free radical biology & medicine, 53(4), 962-973 (2012-05-29)
Complex I is a critical site of O(2)(•-) production and the major host of reactive protein thiols in mitochondria. In response to oxidative stress, complex I protein thiols at the 51- and 75-kDa subunits are reversibly S-glutathionylated. The mechanism of
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