推荐产品
蒸汽密度
4.1 (vs air)
蒸汽壓力
0.02 mmHg ( 20 °C)
化驗
≥99%
形狀
viscous liquid (colorless)
expl. lim.
7.4 %
折射率
n20/D 1.427 (lit.)
bp
197 °C (lit.)
mp
−40 °C (lit.)
密度
0.925 g/mL at 25 °C (lit.)
SMILES 字串
CC(O)CC(C)(C)O
InChI
1S/C6H14O2/c1-5(7)4-6(2,3)8/h5,7-8H,4H2,1-3H3
InChI 密鑰
SVTBMSDMJJWYQN-UHFFFAOYSA-N
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訊號詞
Warning
危險聲明
危險分類
Eye Irrit. 2 - Repr. 2 - Skin Irrit. 2
儲存類別代碼
10 - Combustible liquids
水污染物質分類(WGK)
WGK 1
閃點(°F)
201.2 °F - closed cup
閃點(°C)
94 °C - closed cup
個人防護裝備
Eyeshields, Gloves, type ABEK (EN14387) respirator filter
Structure (London, England : 1993), 18(9), 1210-1219 (2010-09-10)
Enzymatic reactions involving bilayer lipids occur in an environment with strict physical and topological constraints. The integral membrane enzyme PagP transfers a palmitoyl group from a phospholipid to lipid A in order to assist Escherichia coli in evading host immune
Physical chemistry chemical physics : PCCP, 13(8), 3319-3327 (2010-12-25)
The mutual diffusion coefficients for two aqueous ternary systems, both containing a protein, human serum albumin (HSA, component 1), were measured. The first system contained a neutral polymer, polyethylene glycol (PEG, component 2), and the second an "organic solvent", 2-methyl-2,4-pentanediol
Protein science : a publication of the Protein Society, 20(2), 448-456 (2011-02-01)
Staphylococcal α-hemolysin is expressed as a water-soluble monomeric protein and assembles on membranes to form a heptameric pore structure. The heptameric pore structure of α-hemolysin can be prepared from monomer in vitro only in the presence of deoxycholate detergent micelles
Journal of molecular biology, 375(5), 1477-1488 (2007-12-18)
Sodium dodecyl sulfate (SDS) is a highly effective and widely used protein denaturant. We show that certain amphipathic cosolvents such as 2-methyl-2,4-pentanediol (MPD) can protect proteins from SDS denaturation, and in several cases can refold proteins from the SDS-denatured state.
Biochemistry, 45(28), 8599-8606 (2006-07-13)
Kir2.1 channels play a key role in maintaining the correct resting potential in eukaryotic cells. Recently, specific amino acid mutations in the Kir2.1 inwardly rectifying potassium channel have been found to cause Andersen's Syndrome in humans. Here, we have characterized
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