JC polyomavirus capsid viral protein 1 (JCV VP1)

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Experiment Name	JC polyomavirus capsid viral protein 1 (JCV VP1)
Associated Publication	Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif. Neu U, Maginnis MS, Palma AS, Ströh LJ, Nelson CD, Feizi T, Atwood WJ, Stehle T Cell host & microbe, 8, 309-19 2010 Oct 21
Analyte Name	JCV VP1 capsid
Analyte Family	Viral proteins
Analyte Information	Amino acids 22-289 of the Mad-1 strain of JCV VP1 fused to a N-terminal hexa-histidine tag and recombinantly expressed in E. coli. VP1 is the major viral capsid protein and is responsible for virus attachment to host cells and initiation of infection.
Concentration	150 ug/ml
Protocol	After blocking arrayed slides with 0.3% (v/v) Blocker Casein (Pierce), 0.3% (w/v) bovine serum albumin (Sigma A8577) in Hepes buffered saline (5 mM Hepes, pH 7.4, 150 mM NaCl, 5 mM CaCl2), JCV-VP1 was precomplexed with mouse monoclonal anti-poly-histidine and biotinylated anti-mouse IgG antibodies (both from Sigma) in a ratio of 4:2:1 (by weight) and overlaid onto the arrays at 150 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