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Z122807

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Sigma-Aldrich® TLC Plates

silica, highly purified matrix, L × W 20 cm × 20 cm

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About This Item

UNSPSC Code:
41115711
eCl@ss:
32110504

material

polyester support
silica, highly purified matrix

feature

binder Gypsum/polymeric
fluorescent indicator

manufacturer/tradename

Sigma-Aldrich

technique(s)

thin layer chromatography (TLC): suitable

L × W

20 cm × 20 cm

layer thickness

250 μm

plate L × W

20 cm × 20 cm

particle size

17 μm

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General description

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

Application

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

Other Notes

this product will be discontinued, please find the alternative product here :
100390

Legal Information

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

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number

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The Journal of biological chemistry, 282(30), 21583-21587 (2007-06-08)
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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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