67190
1,2,3-庚三醇 溶液
别名:
1,2,3-Heptanetriol solution, Additive Screening Solution 09/Kit-No 78374
InChI
1S/C7H16O3/c1-2-3-4-6(9)7(10)5-8/h6-10H,2-5H2,1H3
SMILES string
CCCCC(O)C(O)CO
InChI key
HXYCHJFUBNTKQR-UHFFFAOYSA-N
density
1.01 g/mL at 20 °C
storage temp.
2-8°C
存储类别
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
法规信息
新产品
此项目有
P Gast et al.
European journal of biochemistry, 239(3), 805-809 (1996-08-01)
Detergent-free reaction centers from Rhodobacter sphaeroides R26 were used to study the solubilization of reaction centers in various detergents and their effects on reaction center photochemistry. 500 +/- 100 n-octyl-beta-D-glucopyranoside or 51 +/- 5 Triton X-100 molecules were associated with
P A Timmins et al.
FEBS letters, 280(1), 115-120 (1991-03-11)
The presence of small amphiphiles has been found to be necessary in the crystallization of several membrane-protein/surfactant complexes. It has been suggested that the role of the small amphiphile may be to reduce the size of the surfactant belt around
T Okada et al.
Journal of structural biology, 130(1), 73-80 (2000-05-12)
Rhodopsin, a prototypic G protein-coupled receptor responsible for absorption of photons in retinal rod photoreceptor cells, was selectively extracted from bovine rod outer segment membranes, employing mixed micelles of nonyl beta-d-glucoside and heptanetriol. Highly purified rhodopsin was crystallized from solutions
J P Allen
Proteins, 20(3), 283-286 (1994-11-01)
The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent beta-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using
M A Rosenow et al.
Acta crystallographica. Section D, Biological crystallography, 59(Pt 8), 1422-1428 (2003-07-24)
The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein
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