Resistin Rat, His
Description
Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid residues of the Resistin Rat and 16 additional amino acid residues – His Tag (underlined).
Product Specs
Resistin, encoded by the RSTN gene, is a peptide hormone classified as a cysteine-rich secreted protein. This family, known as the RELM family, is characterized by the presence of 11 cysteine residues in their monomeric peptide structure. Resistin is also recognized by alternative names such as ADSF (Adipose Tissue-Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone 3). In mice, resistin is initially produced as a 114 amino acid prepeptide. Before secretion, a hydrophobic signal peptide consisting of the N-terminal 20 amino acids is cleaved. The resulting mature mouse resistin protein circulates in the bloodstream as a homodimer. Each monomer of this homodimer comprises 94 amino acids, and the two monomers are connected by a disulfide bond formed between Cys26 residues.
Resistin is thought to play a crucial role in the pathogenesis of obesity. Studies suggest that mouse resistin, primarily produced and released by adipocytes (fat cells), can interact with skeletal muscle cells, liver cells (hepatocytes), and adipocytes themselves. This interaction appears to decrease the sensitivity of these cells to insulin, a hormone essential for regulating blood sugar levels. Research by Steppan et al. has indicated that resistin can impede the process of glucose uptake stimulated by insulin. Furthermore, their findings suggest that resistin levels are elevated in the bloodstream of obese mice and that these levels can be lowered by fasting and treatment with antidiabetic medications. Conversely, Way et al. have reported that resistin expression is significantly reduced in obesity.
Additional studies have demonstrated that mouse resistin levels increase during the differentiation of adipocytes. However, resistin also seems to have an inhibitory effect on adipogenesis, the process of new adipocyte formation. In contrast, the differentiation of human adipocytes appears to be linked to a decrease in resistin gene expression.
Product Science Overview
Resistin, also known as adipose tissue-specific secretory factor (ADSF) or found in inflammatory zone 3 (FIZZ3), is a cysteine-rich peptide hormone. It belongs to the family of resistin-like molecules (RELMs) and is primarily secreted by adipose tissue in rodents . In humans, resistin is predominantly expressed in immune cells . The recombinant form of resistin, tagged with a histidine (His) tag, is used extensively in research to study its biological functions and potential therapeutic applications.
Resistin is composed of 94 amino acids in rodents and 108 amino acids in humans . The structure of resistin includes a carboxy-terminal disulfide-rich β-sandwich “head” domain with positive electrostatic surfaces and an amino-terminal α-helical “tail” segment with negative electrostatic potential . The His tag, consisting of six histidine residues, is added to facilitate purification and detection of the recombinant protein.
Resistin was initially proposed as a link between obesity and diabetes in mice due to its role in promoting insulin resistance . However, its functions extend beyond metabolic regulation. Resistin is now recognized as a pro-inflammatory molecule involved in various chronic inflammatory diseases, metabolic disorders, infectious diseases, and cancers . It also functions as a host defense peptide with broad-spectrum antimicrobial activity and immunomodulatory properties .
Recombinant resistin is typically produced using bacterial expression systems such as Escherichia coli. The gene encoding resistin is cloned into an expression vector, which is then introduced into the bacterial cells. The bacteria are cultured, and the recombinant protein is expressed and accumulated within the cells. The His tag allows for easy purification of the protein using affinity chromatography techniques .
Resistin undergoes various post-translational modifications, including disulfide bond formation, which is crucial for its structural stability and function . The protein’s interactions with other molecules, such as its binding to toll-like receptor 4 (TLR4), play a significant role in mediating its pro-inflammatory effects . Analytical techniques such as SDS-PAGE, mass spectrometry, and ELISA are commonly used to study resistin’s structure, function, and interactions .
The expression and release of resistin are regulated by various factors, including cytokines, hormones, and environmental stimuli . In adipose tissue, resistin expression is influenced by nutritional status and inflammatory signals. In immune cells, resistin production is modulated by microbial products and immune mediators . Understanding these regulatory mechanisms is essential for developing therapeutic strategies targeting resistin-related pathways in diseases.
