Leptin Antagonist Triple Mutant Human Recombinant ( Leptin tA Human )

Catalog # PT_41379

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$201.00
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
Product Size: 10ug
Quantity

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 A
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 s
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
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