C-terminal family 4 CBM from Thermotoga maritima Lam16A laminarinase

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Experiment Name	C-terminal family 4 CBM from Thermotoga maritima Lam16A laminarinase
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	TmCBM4-2
Analyte Family	Carbohydrate-binding modules
Analyte Information	Amino acids 488-643 of the Lam16A C-terminal domain that contains the family 4 CBM, fused to an N-terminal hexa-histidine tag and recombinantly expressed in Escherichia coli. Lam16A modular enzyme from the hyperthermophilic Thermotoga maritima is an extracellular enzyme that was shown to have beta1,3-glucanase (laminarinase) activity.
Concentration	2 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), TmCBM4-2 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 2 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