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CERTIFICATE OF ANALYSIS AND DATA SHEET

PRODUCT DESCRIPTION:
Recombinant ovine leptin, one polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, oLEP was mutated, resulting in L39A/D40A/F41A/I42A mutant was purified by proprietary chromatographic techniques.

SOURCE:
Escherichia Coli.

FORMULATION:
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

PURITY:
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by reducing and non-reducing SDS-PAGE gel.

STORAGE:
Lyophilized oLEP mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 oLEP mutant mg/ml and up to 2 mM and filter sterilization oLEP 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.

SOLUBILITY:
It is recommended to reconstitute the lyophilized oLEP mutant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

BIOLOGICAL ACTIVITY:
oLEP quadruple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of ovine leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

 
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