SCAND1 contains a SCAN box domain, which is a conserved leucine-rich motif approximately 60 amino acids in length. This domain is involved in protein-protein interactions. Unlike the majority of other SCAN domain-containing proteins, SCAND1 does not contain a zinc finger motif . The SCAN box domain facilitates interactions with other proteins such as ZNF38, ZNF191, and MZF-1. Additionally, SCAND1 interacts with ZNF202 and PPARgamma, suggesting its involvement in the transcriptional regulation of genes related to energy homeostasis and lipid metabolism .
Recombinant SCAND1 is typically produced in E. coli expression systems. The recombinant protein often includes an N-terminal His-tag to facilitate purification. For example, a recombinant human SCAND1 protein corresponding to amino acids 1-179 has been expressed in E. coli and purified using conventional chromatography techniques . The purity of the recombinant protein is generally greater than 90%, as determined by SDS-PAGE .
Recombinant SCAND1 is used in various research applications, including blocking experiments with corresponding antibodies. In immunohistochemistry (IHC), immunocytochemistry (ICC), and Western blot (WB) experiments, a 100x molar excess of the protein fragment control is recommended based on the concentration and molecular weight . This recombinant protein is also used to study protein-protein interactions and the transcriptional regulation mechanisms in which SCAND1 is involved.