- Leptin inhibits food intake and stimulates energy expenditure. Leptin also has thermogenic actions and regulates enzymes of the fatty acid oxidation. Severe hereditary obesity in rodents and humans is caused by defects in leptin production. In addition to its critical role in the physiological regulation of body weight, leptin has a variety of other physiological and pathological functions resembling those of cytokines. These functions include the regulation of hematopoiesis, angiogenesis, wound healing, inflammation and immune responses. Recombinant human Leptin produced in E. coli is a single, non-glycosylated polypeptide chain of 147 amino acids and a molecular mass of 16,240 Dalton.
- Product Overview
- Human LEP expressed in E.coli
- CAT# CSC-CTK0606-1 (1 mg); CAT# CSC-CTK0606-5 (5 mg)
- Greater than 95% as determined by SDS-PAGE, FPLC and RP-HPLC analysis.
- Recombinant human Leptin is fully biologically active when compared to standards. Biological activity was determined by inducing proliferation of BaF3 cells stably transfected with the long form of human leptin receptor.
- Endotoxin Level
- Less than 1 EU/μg.
- Sterile-filtered, white, lyophilized (freeze-dried) powder. Lyophilized from a concentrated (1 mg/ml), sterile solution with 0.0045 mM NaHCO3.
- Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.1-1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
- Storage & Stability
- The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu Leptin should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze-thaw cycles.
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