Human resistin is composed of 108 amino acids as a prepeptide, with its hydrophobic signal peptide cleaved before secretion . The mature form of resistin circulates in the blood as a dimeric protein, consisting of two 92 amino acid polypeptides linked via disulfide bonds at Cys26 . Resistin has been implicated in linking obesity to insulin resistance, as it is found at elevated levels in the blood of obese individuals .
The Resistin Mutant (Human Recombinant) is a modified form of the natural resistin protein. This mutant has a specific cysteine residue mutated to prevent dimerization, which may allow it to act as an antagonist . The recombinant form of this protein is produced in Escherichia coli and consists of 93 amino acid residues, with a molecular weight of approximately 9.9 kDa .
Resistin plays a significant role in various physiological and pathological processes. In mice, resistin is produced and secreted by adipocytes and acts on skeletal muscle myocytes, hepatocytes, and adipocytes to reduce their sensitivity to insulin . In humans, resistin is primarily expressed in immune cells and is considered a pro-inflammatory molecule . It has been associated with chronic inflammatory diseases, metabolic disorders, infectious diseases, and certain cancers .
Research on resistin and its mutant forms continues to provide insights into its biological functions and potential therapeutic applications. The resistin mutant, due to its altered structure, may offer new avenues for studying the mechanisms of insulin resistance and inflammation . Additionally, understanding the role of resistin in host defense mechanisms could lead to the development of novel antimicrobial agents .