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’s primary target is the hypothalamus in the brain, where it helps to regulate appetite and energy expenditure.
The Leptin Antagonist Triple Mutant (Rat Recombinant) is a specially engineered variant of the leptin protein. This mutant 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 mass of this protein is approximately 16 kDa . The antagonist is characterized by three specific mutations: L39A, D40A, and F41A . These mutations are crucial for its function as they significantly reduce the binding affinity of leptin to its receptor, thereby inhibiting its action.
To enhance its stability and solubility, the Leptin Antagonist Triple Mutant is 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 mass of approximately 35.6 kDa . This modification helps to increase the half-life of the protein in biological systems and reduces immunogenicity.
The Leptin Antagonist Triple Mutant is used in various research applications to study the physiological and pathological roles of leptin. It is particularly useful in investigating leptin’s effects on appetite regulation, energy expenditure, and its involvement in obesity and metabolic disorders . By inhibiting leptin’s action, researchers can better understand the mechanisms underlying leptin resistance and develop potential therapeutic strategies for related conditions.