Purity: > 90% by SDS - PAGE Format: Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 2mM DTT, 20% glycerol, 100mM NaCl. SNIP1 is smad nuclear interacting protein contains a forkhead-associated (FHA) domain and acts as a nuclear inhibitor of CBP/p300. This protein is an inhibitor of the TGF-beta signal transduction pathway and to be important in suppressing transcriptional activation dependent on the co-activators CBP and p300. Inhibition of NF-kappa B activity is a function of the N-terminal domain of SNIP1 and involves competition of SNIP1 and the NF-kappa B subunit, RelA/p65, for binding to p300, similar to the mechanism of inhibition of Smad signaling by SNIP1. Recombinant human SNIP1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.