Zaloguj się, aby wyświetlić ceny organizacyjne i kontraktowe.
Wybierz wielkość
Zmień widok
Informacje o tej pozycji
Wzór empiryczny (zapis Hilla):
C12H9F3O3
Numer CAS:
Masa cząsteczkowa:
258.19
PubChem Substance ID:
UNSPSC Code:
12352204
Beilstein/REAXYS Number:
8555209
MDL number:
Pomoc techniczna
Potrzebujesz pomocy? Nasz zespół doświadczonych naukowców chętnie Ci pomoże.
Pozwól nam pomócassay
≥98.0% (TLC)
solubility
DMF: soluble, DMSO: soluble, methanol: soluble
fluorescence
λex 333 nm; λem 415 nm in methanol
suitability
suitable for fluorescence
SMILES string
CCOc1ccc2c(OC(=O)C=C2C(F)(F)F)c1
InChI
1S/C12H9F3O3/c1-2-17-7-3-4-8-9(12(13,14)15)6-11(16)18-10(8)5-7/h3-6H,2H2,1H3
InChI key
OLHOIERZAZMHGK-UHFFFAOYSA-N
Other Notes
Substrate for monitoring the activity of cytochrome P450
Ta strona może zawierać tekst przetłumaczony maszynowo.
Klasa składowania
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Wybierz jedną z najnowszych wersji:
Masz już ten produkt?
Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Thomas Van Leeuwen et al.
Pest management science, 62(5), 425-433 (2006-03-22)
Tetranychus urticae Koch has recently developed resistance to chlorfenapyr in Australia and Japan, but no attempt has yet been made to describe the biochemical mechanisms involved in chlorfenapyr resistance. In this study a laboratory-selected chlorfenapyr-resistant strain was investigated. Resistance to
Maori Mitsuda et al.
Protein expression and purification, 46(2), 401-405 (2005-11-29)
Improvement of CYP2B6 expression was examined by co-expression with molecular chaperones GroES/EL. Although a CO-reduced difference spectrum was not detected in Escherichia coli transformed only by the CYP2B6-expressing vector, co-expression of GroES/EL resulted in high-level expression which reached over 2000
Emily E Scott et al.
Chemical research in toxicology, 15(11), 1407-1413 (2002-11-20)
Until recently, all known structures of bacterial cytochromes P450 suggested that substrate access to the buried active site occurred via the F-G region, a surface loop distal to the heme cavity. However, the structure of P450 51 indicates a large