Leptin is a hormone predominantly made by adipose cells and enterocytes in the small intestine that helps to regulate energy balance by inhibiting hunger. It is often referred to as the “satiety hormone” or “fat hormone.” Leptin plays a crucial role in body weight regulation and metabolism.
The Leptin Antagonist Triple Mutant (Mouse Recombinant) is a modified form of the leptin protein. This recombinant protein is designed to inhibit the action of leptin, making it a valuable tool for studying leptin’s role in various physiological processes.
The Leptin Antagonist Triple Mutant is a single non-glycosylated polypeptide chain containing 146 amino acids, with an additional alanine at the N-terminus. The molecular weight of this protein is approximately 16 kDa . The antagonist is created by introducing three specific mutations in the leptin protein: L39A, D40A, and F41A . These mutations significantly reduce the binding affinity of leptin to its receptor, thereby inhibiting its biological activity.
To enhance the stability and solubility of the Leptin Antagonist Triple Mutant, it is often PEGylated. PEGylation involves the attachment of polyethylene glycol (PEG) molecules to the protein. In this case, a 20 kDa mono-PEG is attached to the N-terminus of the protein, resulting in a combined molecular weight of approximately 35.6 kDa . The PEGylated form runs as a 48 kDa protein on SDS-PAGE due to the added mass of the PEG molecule .
The Leptin Antagonist Triple Mutant is used in various research applications to study the role of leptin in metabolism, obesity, and related disorders. It is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of the human leptin receptor . Additionally, it inhibits various leptin effects in several in vitro bioassays .