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Micronemal protein 1 of Neospora caninum (NcMIC1)

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(Asterisks that follow the names of certain probes indicate that predominant components are shown.)

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Experiment NameMicronemal protein 1 of Neospora caninum (NcMIC1)
Associated PublicationMembers of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites.
Friedrich N, Santos JM, Liu Y, Palma AS, Leon E, Saouros S, Kiso M, Blackman MJ, Matthews S, Feizi T, Soldati-Favre D
The Journal of biological chemistry, 285, 2064-76
2010 Jan 15
Analyte NameNeospora caninum MIC1
Analyte FamilyOther microbial proteins
Analyte InformationAmino acids 17-259 in NcMIC1 fused to a N-terminal hexahistidine-thioredoxin tag, nd recombinantly expressed in E. coli.
Concentration20 ug/ml
ProtocolAfter blocking arrayed slides with 1% (w/v) bovine serum albumin (Sigma A8577) in Blocker Casein (Pierce) and 5 mM CaCl2, NcMIC1 was assayed pre-complexed with mouse monoclonal anti-poly-histidine and biotinylated anti-mouse IgG antibodies (both from Sigma) in a ratio of 1:2.5:2.5 (by weight) and overlaid onto the arrays at 20 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 CommentsNA