Xenopus laevis Malectin_5 ug/ml

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Experiment Name	Xenopus laevis Malectin_5 ug/ml
Associated Publication	Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Schallus T, Jaeckh C, Fehér K, Palma AS, Liu Y, Simpson JC, Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C Molecular biology of the cell, 19, 3404-14 2008 Aug
Analyte Name	Xenopus malectin
Analyte Family	Animal lectins
Analyte Information	Amino acids 27-213 of the Xenopus laevis sequence fused to a N-terminal hexa-histidine tag and recombinantly expressed in E. coli. Malectin was first detected in X. laevis but soon found to be highly conserved protein of the endoplasmic reticulum of animals, with a characteristic fold resembling carbohydrate-binding modules of bacterial glycoside hydrolases. Evidence is pointing to a role for malectin in N-glycosylation pathway and quality control of nascent glycoproteins in the ER.
Concentration	5 ug/ml
Protocol	After blocking arrayed slides with 1% (w/v) bovine serum albumin (Sigma A8577) in Pierce Blocker solution (casein/BSA) and 10 mM CaCl2, malectin was precomplexed with mouse monoclonal anti-poly-histidine and biotinylated anti-mouse IgG antibodies (both from Sigma) in a ratio of 1:3:3 (by weight) and overlaid onto the arrays at 5 ug/ml. Binding was detected using Alexa Fluor-647-labeled streptavidin from Molecular Probes (1 ug/ml). As diluent the blocker solution was used.
Other Comments	NA