Recombinant Human CYP26B1 protein

CYP26B1 is a member of the cytochrome P450 superfamily, specifically classified under the CYP26 subfamily, which plays a critical role in the metabolism of retinoic acid (RA), an active derivative of vitamin A. As a key regulatory enzyme, CYP26B1 catalyzes the hydroxylation of RA into inactive metabolites, thereby tightly controlling its intracellular concentration. This precise regulation is vital for maintaining cellular homeostasis, as RA acts as a potent signaling molecule involved in embryonic development, cellular differentiation, and tissue morphogenesis. Dysregulation of CYP26B1 has been linked to developmental abnormalities, skin disorders, and cancer, highlighting its physiological and pathological significance.

Recombinant CYP26B1 protein is produced using biotechnological methods, typically through heterologous expression in systems like bacterial (E. coli), yeast, or mammalian cell lines. The recombinant form retains the enzymatic activity of the native protein, enabling researchers to study its structure, substrate specificity, and interaction with inhibitors or modulators in vitro. Its production often involves codon optimization, affinity tag fusion (e.g., His-tag), and purification via chromatography to ensure high purity and functionality.

Research applications of recombinant CYP26B1 span drug discovery and toxicology. It is used to screen potential inhibitors targeting RA metabolism, which could have therapeutic value in cancers or dermatological conditions driven by RA imbalance. Additionally, it aids in studying genetic polymorphisms affecting enzyme activity and their association with disease susceptibility. Structural studies using recombinant protein have also contributed to understanding its catalytic mechanism and designing targeted therapies. Overall, CYP26B1 recombinant protein serves as a crucial tool for unraveling RA-mediated pathways and developing precision medicine approaches.