Leptin Antagonist Triple Mutant, Rat Recombinant, is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant, Rat Recombinant, was purified by proprietary chromatographic techniques.
Formulation: The Rat Leptin triple anatagonist was lyophilized from a concentrated (0. 65mg/ml) solution with 0.003mM NaHCO3.
Physical Appearance: White lyophilized (freeze-dried) powder.
Purity: Greater than 99% as determined by: (a) Gel filtration analysis. (b) Analysis by SDS-PAGE.
Solubility: It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant in sterile water or sterile 0. 4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Stability: Lyophilized Leptin Antagonist Triple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at +4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Biological Activity: Leptin Antagonist Triple Mutant half-life in circulation after SC injection was over 20 hours. Leptin Antagonist Triple Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.
Source:Escherichia coli. Protein content: Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. 0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
Transportation method: Shipped at Room temperature
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