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Sigma-Aldrich® TLC Plates

chiral-silica gel matrix, L × W 20 cm × 20 cm, binder, Polymeric, fluorescent indicator: no

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About This Item

Código UNSPSC:
41115711
eCl@ss:
32110504

Materiais

chiral-silica gel matrix
glass support

Características

binder Polymeric
fluorescent indicator: no

fabricante/nome comercial

Sigma-Aldrich

técnica(s)

thin layer chromatography (TLC): suitable

C × L

20 cm × 20 cm

espessura da camada

250 μm

tamanho de partícula

10 μm

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Descrição geral

Thin-layer chromatography (TLC) plates for adsorption, partition, and ion-exchange techniques. Six media choices with glass, polyester, and aluminum backings. Silica-based adsorbent layers in Sigma-Aldrich TLC plates incorporate a polymeric binder; highly purified silica gel plates incorporate a gypsum/polymer binder.
  • Silica gel - for weakly to strongly polar separations, pore size 60 Å
  • High purity silica gel - acid washed for separation of aflatoxins
  • Cellulose - for partition chromatography, (SigmaCell Type 100 Cellulose)
  • Cellulose PEI - for separation of weak anions (amino acids, peptides) PEI plates may turn slightly yellow, affecting separation. Pre-develop plates in distilled water to minimize yellow color.
  • Chiral silica - for separation of optically active isomers by ligand exchange, pore size 60Å

Aplicação

Sigma-Aldrich® TLC Plates was used for TLC analysis during GTPase activity assay and lipid extraction/analysis.

Informações legais

SIGMA-ALDRICH is a registered trademark of Merck KGaA, Darmstadt, Germany

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Chuang-Rung Chang et al.
The Journal of biological chemistry, 282(30), 21583-21587 (2007-06-08)
Mitochondria in cells comprise a tubulovesicular reticulum shaped by dynamic fission and fusion events. The multimeric dynamin-like GTPase Drp1 is a critical protein mediating mitochondrial division. It harbors multiple motifs including GTP-binding, middle, and GTPase effector (GED) domains that are
Heiko Runz et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 22(5), 1679-1689 (2002-03-07)
Generation of amyloid-beta (Abeta) from the amyloid precursor protein (APP) requires proteolytic cleavage by two proteases, beta- and gamma-secretase. Several lines of evidence suggest a role for cholesterol on secretase activities, although the responsible cellular mechanisms remain unclear. Here we

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