Plant/Algal cell antibodies / Oryza sativa

product information

This antibody specifically cross-reacts against fucose residues bound to the protein N-glycans in alpha 1,3. This residue is characterisitc of the plant protein N-glycans and is absent in protein N-glycans from animals. This residue is added in the Golgi apparatus.

core fucose residues bound to the N-glycan in alpha 1,3

store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

western blot (WB)

AS07 267 | anti-xylose rabbit antibody

Alpha (1,3) fucose is present not only in plants but also in some invertebrates (such as nematodes, bees, etc.) . However, cross-reaction with glycoproteins from these organisms is weaker than the one observed in plants. This sugar residue does not exist in mammals, in their endogenous glycoproteins.

application information

1 ug/10 ml of incubation buffer, with standard ECL (WB)

10 - 100 for various glycoproteins

higher plants

higher plants

no confirmed exceptions from predicted reactivity known in the moment

controls:

PLA2 (phospholipase 2 from bee venom) which contains only α1.3 fucose, Sigma, product number P9279

Type II - horseradish peroxidase which contains β1.2 Xylose and α1.3 fucose, Sigma, product number P8250

The antibody does not recognize alpha 1,6-fucose.

Baiet et all. (2010). N-glycans of Phaeodactylum tricornutum diatom and functional characterization of its N-acetylglucosaminyltransferase I enzyme. J Biol. Chem. Dec 17.

application example

Total cell extract from Arabidopsis thaliana wild type (1) and cell extracts from different mutants defective in fucosyltransferases (2-5) (data not published yet).

Primary antibody has been used at 10 µg/10 ml of incubation buffer. Detection has been done using ECL.

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