Streptococcus pneumoniae Hyaluronan-specific Carbohydrate-binding Module

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Experiment Name	Streptococcus pneumoniae Hyaluronan-specific Carbohydrate-binding Module
Associated Publication	Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module. Suits MDL, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston AB The Journal of biological chemistry, 289, 27264-27277 2014 Sep 26
Analyte Name	His-HysACBM or SpCBM70
Analyte Family	Carbohydrate-binding modules
Analyte Information	N-terminal carbohydrate-binding module domain (CBM) of the hyaluronate lyase (Hyl) from Streptococcus pneumoniae. The CBM is the founder member of CBM family 70 and named SpCBM70. Amino acids 53-212 comprising the CBM domain were fused to an N-terminal hexa-histidine tag and recombinantly expressed in Escherichia coli. The recognition and degradation of host hyaluronan by Hyl contributes to bacterial spreading through the extracellular matrix and enhancing access to host cell surfaces.
Concentration	10 ug/ml
Protocol	After blocking arrayed slides with 3% w/v bovine serum albumin (Sigma A8577) in Hepes buffered saline (5 mM Hepes, pH 7.4, 150 mM NaCl, 5 mM CaCl2), SpCBM70 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 10 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	N/A