Human SERTA domain-containing protein 2 ( SERTAD2, also know as TRIP-Br2 ) is a member of a novel family of mammalian transcriptional co-regulators comprised of five members, four of which have been shown to modulate E2F-dependent transcriptional activities. In adipose tissue, TRIP-Br2 plays a role in fat lipolysis & thermogenesis by recruiting PHD zinc finger- and/or bromodomain-containing transcriptional co-regulators, such as p300/CBP and KRIP-1, to E2F1/DP1 transcription complexes assembled on E2F-responsive promoters. In E2F/DP1 pathway, TRIP-Br2 regulates adipocyte biology and energy metabolism. Recent evidence also suggests that besides TRIP-Br2’s roles in cell cycle regulation, fat energy metabolism, its Drsophila homolog protein “TARANIS” is molecule, which regulates normal sleep pattern.

Full-length human TRIP-Br2 (313aa, derived from BC074789) gene was constructed using gene synthesis technology with codon optimization. 31 aa (T7 / His / TEV cleavage site) Tag was fused to LMX1B N-terminal. This protein was expressed in E.coli as inclusion bodies. It was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro TRIP-Br2 mediated gene transcription regulation study for neuronal cell sleep cycle pathway and cancer cell’s lipolysis, thermogenesis regulation with “ProFectin” reagent based intracellular delivery of this protein.

2. May be used as specific protein substrate for kinase and ubiquitin (Sumo pathway) related enzyme functional screening assays.

3. May be used for TRIP-Br2 protein-protein interaction mapping.

4. Potential diagnostic biomarker protein, which could be used for monitoring various cancer cell progression.

5. As immunogen for specific antibody production.