Recombinant Human Leptin - rHuLeptin



Data Sheet
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Recombinant Human Leptin - rHuLeptin

Description Recombinant Human Leptin produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16,240 Dalton. The rHuLeptin is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Solubility: The lyophilized rHuLeptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
Stability: Lyophilized rHuLeptin although stable at room temperature, should be stored desiccated below 0 °C. Reconstituted rHuLeptin is best stored refrigerated at 4 °C.
Purity: Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
Amino acid sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Met-Val-Pro-Ile-Gln.
Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
Biological Activity: ProSpec's rHuLeptin is fully biologically active when compared to standards. The ED50, calculated by the leptin-dependant stimulation of Human OB-R transfected murine BaF3 indicator cells is 0.5-1.6 ng/ml.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rHuLeptin.
Protein content: Protein quantitation was carried out by two independent methods: UV spectroscopy at 280 nm using the absorbency value of 0.878 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). Analysis by RP-HPLC, using a calibrated solution of Leptin as a Reference Standard.
Usage This material is for research, laboratory or further manufacturing purposes.