Micronemal protein 1 of Toxoplasma gondii (TgMIC1)_(2010 data)

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Experiment Name	Micronemal protein 1 of Toxoplasma gondii (TgMIC1)_(2010 data)
Associated Publication	Members 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 Name	T. gondii MIC1
Analyte Family	Other microbial proteins
Analyte Information	Amino acids 17-262 in TgMIC1 fused to a N-terminal hexahistidine-thioredoxin tag, and recombinantly expressed in E. coli. TgMIC1 is one of the first micronemal proteins to be discovered in T. gondii, which functions in cell adhesion and has an important role for early stages of host-cell invasion.
Concentration	40 ug/ml
Protocol	After blocking arrayed slides with 1% (w/v) bovine serum albumin (Sigma A8577) in Blocker Casein (Pierce) and 5 mM CaCl2, TgMIC1 was precomplexed 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 40 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