Recombinant human Leptin Antagonist Triple Mutant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant was purified by proprietary chromatographic techniques.
Formulation: The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045 mM NaHCO3.
Physical Appearance: White lyophilized (freeze-dried) powder.
Purity: Greater than 98% as determined by: (a) Gel filtration analysis. (b) Analysis by SDS-PAGE.
Source:Escherichia coli. Amino acid sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Uniprot ACC number:Transportation method: Shipped at room temperature.
Stability: Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin 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: ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several
in vitro bioassays.
Solubility: It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
References: Title: Leptin-induced vascular smooth muscle cell proliferation via regulating cell cycle, activating ERK1/2 and NF-kB Publication: Acta biochimica et biopH ysica Sinica 42.5 (2010): 325-331. Link: http://abbs. oxfordjournals. org/content/42/5/325. full
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