Human malectin

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Experiment Name	Human malectin
Associated Publication	Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin. Palma AS, Liu Y, Muhle-Goll C, Butters TD, Zhang Y, Childs R, Chai W, Feizi T Methods in enzymology, 478, 265-86 2010
Analyte Name	Human 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	Full laser power scan was used to highlight the binding of malectin to the glucan oligosaccharide sequences. Under this setting the binding signal to the Glc2-N-glycan probe was too high (saturated) to be accurately quantified.