The mutant form of prolactin antagonist, specifically the R129G mutant, is characterized by a truncation of nine amino acids from its N-terminus. This truncation enhances its inhibitory activity compared to the wild-type prolactin . The molecular mass of this recombinant protein is approximately 23 kDa .
The amino acid sequence of the first five N-terminal residues of the prolactin antagonist is Ala-Thr-Pro-Val-Cys-Pro . The protein is typically lyophilized from a concentrated solution containing 0.02%-0.03% sodium bicarbonate (NaHCO3) and is greater than 99.0% pure as determined by gel filtration and SDS-PAGE .
The prolactin antagonist mutant form is devoid of agonistic activity, meaning it does not activate prolactin receptors. Instead, it effectively inhibits the biological activity of ovine prolactin (oPRL) and other lactogenic hormones. This inhibition has been demonstrated through proliferation assays using Nb2 cells and other cell lines .
Prolactin antagonists are valuable tools in research and therapeutic applications. They can be used to study the physiological roles of prolactin and to develop treatments for conditions associated with excessive prolactin activity, such as prolactinomas (prolactin-secreting tumors) and hyperprolactinemia (elevated levels of prolactin in the blood).
The production of prolactin antagonist ovine recombinant, mutant involves recombinant DNA technology. The gene encoding the mutant prolactin is inserted into E. coli cells, which then express the protein. The recombinant protein is subsequently purified using proprietary chromatographic techniques to achieve high purity and activity .
The lyophilized form of the protein is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage. Upon reconstitution, the protein should be stored at 4°C for short-term use and below -18°C for future use. It is recommended to add a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), to prevent freeze-thaw cycles .