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추천 제품
Grade
reagent grade
vapor density
4.55 (vs air)
vapor pressure
0.18 mmHg ( 20 °C)
분석
≥97%
autoignition temp.
723 °F
expl. lim.
0.8 %, 100 °F
5 %, 150 °F
refractive index
n20/D 1.541 (lit.)
bp
207 °C (lit.)
mp
−35 °C (lit.)
density
0.973 g/mL at 25 °C (lit.)
SMILES string
C1CCc2ccccc2C1
InChI
1S/C10H12/c1-2-6-10-8-4-3-7-9(10)5-1/h1-2,5-6H,3-4,7-8H2
InChI key
CXWXQJXEFPUFDZ-UHFFFAOYSA-N
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법적 정보
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Aquatic Chronic 2 - Asp. Tox. 1 - Carc. 2 - Eye Irrit. 2 - Skin Irrit. 2
보충제 위험성
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point (°F)
159.8 °F - closed cup
Flash Point (°C)
71 °C - closed cup
Bin Ma et al.
Bioorganic & medicinal chemistry letters, 20(7), 2264-2269 (2010-03-02)
Modifying FTY720, an immunosuppressant modulator, led to a new series of well phosphorylated tetralin analogs as potent S1P1 receptor agonists. The stereochemistry effect of tetralin ring was probed, and (-)-(R)-2-amino-2-((S)-6-octyl-1,2,3,4-tetrahydronaphthalen-2-yl)propan-1-ol was identified as a good SphK2 substrate and potent S1P1
Laura Ledesma García et al.
The Journal of biological chemistry, 286(3), 1709-1718 (2010-11-12)
Previous genetic studies in Sphingomonas macrogolitabida strain TFA have established that expression of genes involved in tetralin biodegradation (thn genes) requires the function of the LysR type activator ThnR and also ThnY. Sequence comparison indicated that ThnY is homologous to
Laura Tomás-Gallardo et al.
Applied and environmental microbiology, 78(15), 5460-5462 (2012-05-29)
Glucose catabolite repression of tetralin catabolic genes in Rhodococcus sp. strain TFB was shown to be exerted by a protein homologous to transcriptional regulators of the cyclic AMP receptor (CRP)-FNR family. The protein was detected bound to putative CRP-like boxes
Laura Tomás-Gallardo et al.
Microbial biotechnology, 2(2), 262-273 (2009-03-01)
The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram-positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin- and glucose-grown cells was compared using the 2D-DIGE technique.
Jordi Casanovas et al.
Bioorganic chemistry, 33(6), 484-492 (2005-11-18)
The conformational properties of polygamain and morelensin, two aryltetralin lignan lactones, have been investigated in both the gas-phase and chloroform solution using DFT calculations at the B3LYP/6-311G(d,p) level. Results indicate that the conformation of polygamain is very rigid. Thus, the
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