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Merck
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Documenti fondamentali

50791

Sigma-Aldrich

1,2,3-Heptanetriol Isomer H 0.5 solution

Sinonimo/i:

1,2,3-Heptanetriol solution, Additive Screening Solution 08/Kit-No 78374

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About This Item

Numero CAS:
Numero MDL:
Codice UNSPSC:
12352200
ID PubChem:

Temperatura di conservazione

2-8°C

Stringa SMILE

CCCCC(O)C(O)CO

InChI

1S/C7H16O3/c1-2-3-4-6(9)7(10)5-8/h6-10H,2-5H2,1H3
HXYCHJFUBNTKQR-UHFFFAOYSA-N

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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves


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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
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
Bryan W Berger et al.
Protein science : a publication of the Protein Society, 15(12), 2682-2696 (2006-11-08)
The interactions leading to crystallization of the integral membrane protein bacteriorhodopsin solubilized in n-octyl-beta-D-glucoside were investigated. Osmotic second virial coefficients (B(22)) were measured by self-interaction chromatography using a wide range of additives and precipitants, including polyethylene glycol (PEG) and heptane-1,2,3-triol
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
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

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