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Merck

73033AST

Supelco

Astec® CHIRALDEX G-TA Capillary GC Column

L × I.D. 30 m × 0.25 mm, df 0.12 μm

Szinonimák:

GC column, chiral, gamma-dextran

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
41115710
NACRES:
SB.54

material

fused silica

Minőségi szint

leírás

GC capillary column

kiszerelés

pkg of 1 ea

parameter

-10-180 °C temperature (isothermal or programmed)

Béta-érték

500

df

0.12 μm

technika/technikák

gas chromatography (GC): suitable

H × belső átmérő

30 m × 0.25 mm

mátrix aktív csoport

non-bonded; 2,6-di-O-pentyl-3-trifluoroacetyl derivative of γ-cyclodextrin phase

alkalmazás(ok)

agriculture
chemicals and industrial polymers
cleaning products
clinical
cosmetics
environmental
flavors and fragrances
food and beverages
forensics and toxicology
life science and biopharma
personal care
pharmaceutical (small molecule)

oszloptípus

capillary chiral

elválasztástechnika

chiral

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Általános leírás

Astec® CHIRALDEX G-TA is the first choice in the Group 1 CSPs (Surface Interactions, Complex Derivatives). This phase has been shown to be the most broadly-selective phase for the pharmaceutical industry, especially for the analysis of chiral intermediates and drug studies in various stages of clinical trials. Separations occur without the inclusion mechanism and are typically faster and more efficient than most chiral stationary phases. G-TA has also been used to separate parent drug enantiomers and their metabolites. G-TA has its highest selectivity for oxygen-containing analytes like alcohols, diols and polyols as the free alcohol and as an acyl derivative; amines as acyl derivatives; amino alcohols, halogens (Cl>Br>F), amino acids, hydroxy acids, lactones, furans and pyrans. It is also highly selective for halogenated compounds.

Alkalmazás

Astec® CHIRALDEX G-TA (2,6-di-O-pentyl-3-trifluoroacetyl-γ-cyclodextrin) derivatized cyclodextrin chiral stationary phase may be used in capillary gas chromatography for separation of four isomers from 7 racemic sulfinate esters. It was used in an experimental study done for cloning and characterization of three epoxide hydrolases identified by analyzing open reading frames (ORFs) of a marine bacterium, Erythrobacter litoralis HTCC2594. It was also used in HPLC and GC analyses of the conversion of epoxides during enantioselectivity of epoxide hydrolase from Agrobacterium radiobacter (EchA) using error-prone PCR and DNA shuffling.

Kémiai/fizikai ellenállás

Temp. Limits:
  • -10 °C to 180 °C isothermal and programmed

Egyéb megjegyzések

We offer a variety of chromatography accessories including analytical syringes

Jogi információk

Astec is a registered trademark of Merck KGaA, Darmstadt, Germany
CHIRALDEX is a trademark of Sigma-Aldrich Co. LLC

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Dokumentumtár megtekintése

Jung-Hee Woo et al.
Applied microbiology and biotechnology, 76(2), 365-375 (2007-06-02)
Previously, we reported that ten strains belonging to Erythrobacter showed epoxide hydrolase (EHase) activities toward various epoxide substrates. Three genes encoding putative EHases were identified by analyzing open reading frames of Erythrobacter litoralis HTCC2594. Despite low similarities to reported EHases
Bert van Loo et al.
Chemistry & biology, 11(7), 981-990 (2004-07-24)
The enantioselectivity of epoxide hydrolase from Agrobacterium radiobacter (EchA) was improved using error-prone PCR and DNA shuffling. An agar plate assay was used to screen the mutant libraries for activity. Screening for improved enantioselectivity was subsequently done by spectrophotometric progress
Asymmetric ring opening of meso-epoxides with B-halobis(2-isocaranyl)boranes 2-dIcr2BX
Roy, Chandra D., Brown, Herbert C.
Tetrahedron Asymmetry, 17 (13), 1931-1936 (2006)
Catalytic asymmetric synthesis of Japonilure and its enantiomer
Xu, Hao, et al.
Tetrahedron Asymmetry, 25 (20-21), 1372-1375 (2014)
Hugo L van Beek et al.
FEBS open bio, 4, 168-174 (2014-03-22)
Enzyme stability is an important parameter in biocatalytic applications, and there is a strong need for efficient methods to generate robust enzymes. We investigated whether stabilizing disulfide bonds can be computationally designed based on a model structure. In our approach

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