Greater than 90% as determined by SDS-PAGE.
ApoD is primarily associated with high-density lipoproteins (HDL) in human plasma. It binds to various ligands, including cholesterol, progesterone, pregnenolone, bilirubin, and arachidonic acid . This multifunctional lipid-binding protein is expressed in numerous tissues, with high levels of expression in the spleen, testes, and brain .
ApoD is involved in the maintenance and repair of the central and peripheral nervous systems. It accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions such as Alzheimer’s disease . Additionally, it is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with an increased risk of breast cancer .
Human recombinant ApoD is produced using Escherichia coli (E. coli) as the expression host. The recombinant protein is a single, non-glycosylated polypeptide chain containing 174 amino acids and has a molecular mass of approximately 19.82 kDa . The protein sequence corresponds to the UniProtKB/Swiss-Prot entry P05090 .
To enhance the protein’s solubility and facilitate genetic manipulation, several amino acid exchanges are introduced at the surface of ApoD. These modifications include Trp99His, Cys116Ser, Ile118Ser, Leu120Ser, Leu23Pro, Pro133Val, and Asn134Ala . The recombinant ApoD is purified using proprietary chromatographic techniques to achieve a purity greater than 90% as determined by SDS-PAGE .
Recombinant ApoD has potential therapeutic applications due to its role in lipid metabolism and neuroprotection. It is used in research to study its physiological functions and potential therapeutic benefits . The lyophilized protein is stable when stored at -20°C and can be reconstituted in deionized water to a working volume of 0.5 mg/ml .