Purity: > 90% by SDS - PAGE Format: Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 10% glycerol, 1mM DTT . BCCIP was isolated on the basis of its interaction with BRCA2 and p21 proteins. It is an evolutionarily conserved nuclear protein with multiple interacting domains. The N-terminal half shares moderate homology with regions of calmodulin and M-calpain, suggesting that it may also bind calcium. Functional studies indicate that this protein may be an important cofactor for BRCA2 in tumor suppression, and a modulator of CDK2 kinase activity via p21. This protein has also been implicated in the regulation of BRCA2 and RAD51 nuclear focus formation, double-strand break-induced homologous recombination, and cell cycle progression. Recombinant human BCCIP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.