Herpes virus VP16 activates expression of immediate early genes in virally-infected cells (1). As most other eukaryotic transcriptional activator proteins, VP16 has a modular domain structure: it’s N-terminus is involved in DNA-protein interactions, while it’s C-terminal 79 amino acids have proven to be an especially potent transactivation domain (2). VP16 has been shown to bind to TBP (3), TFIIB (4), and replication factor A (5).
Recombinant GST-VP16 is isolated from an E. coli strain that carries the coding sequence of the fused protein under the control of a T7 promoter.

GST-VP16 has been applied in protein-protein interactions assays.
Protein is greater than 95% homogeneous and based on SDS-PAGE analysis.

1 unit equals 1 nanogram of purified protein. 100 units (ng) are sufficient for a protein-protein interaction assay.
variable in different lots

1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA

References:
1. Post, L.E., et al., (1981) Cell 24, 555-565
2. Triezenberg, S.J., et al., (1988) Genes Dev. 2, 718-729
3. Stringer, K. F., et al., (1990) Nature 345, 783-786
4. Lin, Y-S., et al., (1991) Nature 353, 569-571
5. He, Z., et al., (1993) 73, 1223-1232

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