CBR4 Human

CBR4 is typically expressed in Escherichia coli (E. coli) and is often produced as a recombinant protein. The recombinant form of CBR4 is fused with a 20 amino acid His tag at the N-terminus, resulting in a single, non-glycosylated polypeptide chain containing 257 amino acids and having a molecular mass of approximately 27.5 kDa . The enzyme is purified using proprietary chromatographic techniques to achieve a purity greater than 95% as determined by SDS-PAGE .

CBR4 forms a heterotetramer with HSD17B8, which has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. This activity is essential for the reduction of o- and p-quinones . The homotetramer form of CBR4 exhibits NADPH-dependent quinone reductase activity, demonstrating its versatility in substrate reduction .

The enzyme is typically stored in a Tris-HCl buffer (pH 8.0) containing glycerol, DTT, and NaCl to maintain its stability. For long-term storage, it is recommended to add a carrier protein such as HSA or BSA and to avoid multiple freeze-thaw cycles . The enzyme’s activity and stability are crucial for its application in various biochemical and research settings.

CBR4 is widely used in laboratory research for its role in fatty acid biosynthesis and its ability to reduce a broad range of quinones. Its recombinant form allows for consistent and reliable results in experimental setups. The enzyme’s broad substrate specificity makes it a valuable tool for studying various biochemical pathways and reactions involving quinones .