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Leptin Antagonist Triple Mutant Human Recombinant ( Leptin tA Human )
DescriptionLeptin Antagonist Triple Mutant Human Recombinant 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
Data sheet
| Formulation | The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3. |
| Solubility | It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100ug/ml, which can then be further diluted to other aqueous solutions. |
| Purity | Greater than 98.0% as determined by:(a) Gel filtration analysis.(b) Analysis by SDS-PAGE. |
| Description | Leptin Antagonist Triple Mutant Human Recombinant 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 Human Recombinant was purified by proprietary chromatographic techniques. |
| Expression host | Escherichia coli. |
| Reagent Appearance | White lyophilized (freeze-dried) powder. |
| 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 mM 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. |
| 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. |
| Biological Activity | ProSpecs 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. |
| References | Title: Leptin-induced vascular smooth muscle cell proliferation via regulating cell cycle, activating ERK1/2 and NF-kB Publication: Acta biochimica et biophysica Sinica 42.5 (2010): 325-331. Link: http://abbs.oxfordjournals.org/content/42/5/325.full |