Leptin inhibits food intake and stimulates energy expenditure. Leptin also has thermogenic actions and regulates enzymes of 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 physiologic 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 Rat Leptin produced in E. coli is a single, non-glycosylated, polypeptide chain of 147 amino acids and a molecular mass of 16,240 Dalton.
Rat Lep expressed in E.coli
CAT# CSC-CTK0874-10 (10 μg); CAT# CSC-CTK0874-50 (50 μg)
Greater than 95% as determined by SDS-PAGE, FPLC and RP-HPLC analysis.
Recombinant rat Leptin is fully biologically active when compared to standards. The ED50, calculated by the leptin-dependant stimulation of Human OB-R transfected murine BaF3 indicator cells, is 0.35-0.06 ng/ml.
Less than 1 EU/μg.
Sterile-filtered white, lyophilized (freeze-dried) powder. The protein was lyophilized from a concentrated (1 mg/ml) 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 rRa Leptin should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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