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Leptin Human, N82K

Source: Escherichia Coli.Sterile Filtered White lyophilized (freeze-dried) powder.Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.Leptin N82K Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids (and additional Ala at N-terminus acids) and having a molecular mass of 16kDa. The Leptin N82K is purified by proprietary chromatographic techniques.

Product Specifications

Product Name Alternative

OB Protein, Obesity Protein, OBS, Obesity factor.

Applications

Functional Assay

Purification

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

Components

Lyophilized from a concentrated (1mg/mL) solution with 0.0045mM NaHCO3.It is recommended to reconstitute the lyophilized leptin N82K in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100μg/ml, which can then be further diluted to other aqueous solutions.

Storage Conditions

Lyophilized leptin N82K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) . Please prevent freeze-thaw cycles.

Applications Notes

Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Amino Acids

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

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