Resistin Mouse
Escherichia Coli.
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Description
Resistin Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 95 amino acids and having a total molecular mass of 20.6kDa.
The Resistin is purified by proprietary chromatographic techniques.
Product Specs
Resistin, encoded by the RSTN gene, is a peptide hormone classified as a cysteine-rich secreted protein within the RELM family. It is also known as ADSF (Adipose Tissue-Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin, initially a 108-amino acid prepeptide, undergoes cleavage of its hydrophobic signal peptide before secretion. In human blood, it circulates as a dimer, formed by two 92-amino acid polypeptides linked by a disulfide bond at Cys26.
Resistin is implicated in the connection between obesity and insulin resistance. Produced and secreted by adipocytes, mouse resistin interacts with skeletal muscle myocytes, hepatocytes, and adipocytes, reducing their insulin sensitivity. Steppan et al. propose that resistin inhibits insulin-stimulated glucose uptake and is found at elevated levels in obese mice, with levels decreasing during fasting and with antidiabetic drug treatment. Conversely, Way et al. suggest that resistin expression is suppressed in obesity and upregulated by antidiabetic drugs.
Mouse resistin levels increase during adipocyte differentiation, yet it appears to inhibit adipogenesis. In contrast, human adipogenic differentiation is likely linked to downregulation of resistin gene expression.
Recombinant Mouse Resistin, produced in E. coli, is a non-glycosylated, homodimeric polypeptide chain composed of two chains of 95 amino acids, resulting in a total molecular mass of 20.6 kDa.
Purification of Resistin is achieved using proprietary chromatographic techniques.
Lyophilized from a sterile filtered solution containing 0.1% trifluoroacetic acid (TFA).
For reconstitution, it is recommended to dissolve the lyophilized Resistin in sterile 18 MΩ·cm H2O at a concentration of 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Lyophilized Resistin remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. Upon reconstitution, Mouse Resistin should be stored at 4°C for 2-7 days. For long-term storage, it is advisable to store it below -18°C.
For extended storage, adding a carrier protein (0.1% HSA or BSA) is recommended.
Avoid repeated freeze-thaw cycles.
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Escherichia Coli.
MSSMPLCPID EAIDKKIKQD FNSLFPNAIK NIGLNCWTVS SRGKLASCPE GTAVLSCSCG SACGSWDIRE EKVCHCQCAR IDWTAARCCK LQVAS.
Product Science Overview
Resistin was initially discovered as a link between obesity and diabetes in mice . In murine models, resistin is primarily secreted by adipocytes (fat cells), and its circulating levels increase in various obesity models, leading to insulin resistance . This discovery suggested that resistin might play a significant role in the development of type 2 diabetes mellitus.
Recombinant mouse resistin (rmRetn) has been successfully cloned, expressed, and purified in Escherichia coli . The purification process typically involves ion exchange chromatography, resulting in a high-purity protein with an endotoxin level of less than 1.0 EU/µg . The purified recombinant protein has been shown to possess chemotaxis effects in mouse aortic endothelial cells in vitro .
Resistin has been found to have multiple biological functions, including its role as a pro-inflammatory cytokine . It activates endothelial cell functions, induces the proliferation and migration of smooth muscle cells, and promotes macrophage lipid deposition . These activities suggest that resistin may act as a bridge linking inflammation and insulin resistance .
In addition to its role in metabolism and inflammation, resistin has been implicated in the regulation of hematopoiesis (the formation of blood cellular components) in mice . Studies have shown that recombinant mouse resistin can upregulate the colony-forming unit (CFU) number in bone marrow and protect mice from the chemotoxicity of 5-fluorouracil, a chemotherapy drug .
The discovery of resistin’s role in inflammation and metabolism has significant clinical implications. In humans, resistin is predominantly expressed in immune cells and is considered a pro-inflammatory molecule . It plays a regulatory role in various chronic inflammatory diseases, metabolic disorders, infectious diseases, and cancers . Understanding the functions and mechanisms of resistin can provide new insights into developing therapeutic strategies for these conditions.
