N-terminal family 41 CBM from Thermotoga maritima TmPul13 pullulanase

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Experiment Name	N-terminal family 41 CBM from Thermotoga maritima TmPul13 pullulanase
Associated Publication	Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry. Palma AS, Liu Y, Zhang H, Zhang Y, McCleary BV, Yu G, Huang Q, Guidolin LS, Ciocchini AE, Torosantucci A, Wang D, Carvalho AL, Fontes CM, Mulloy B, Childs RA, Feizi T, Chai W Molecular & cellular proteomics : MCP, 14, 974-88 2015 Apr
Analyte Name	TmCBM41
Analyte Family	Carbohydrate-binding modules
Analyte Information	Amino acids 20-120 of the TmPul13 N-terminal domain that contains the family 41 CBM, fused to an N-terminal hexa-histidine tag and recombinantly expressed in Escherichia coli. TmPul13 modular pullulanase from the hyperthermophilic Thermotoga maritima is a thermostable enzyme that was shown to be specific for the alpha1,6-glucose linkage in pullulan polysaccharide.
Concentration	1 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), TmCBM41 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 1 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