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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. |
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Source |
Escherichia Coli. |
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Physical Appearance: |
Sterile Filtered White lyophilized (freeze-dried) powder.
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Formulation: |
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
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Solubility: |
The lyophilized rHuLeptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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Stability: |
Lyophilized rHuLeptin although stable at room temperature, should be stored desiccated below 0 °C. Reconstituted rHuLeptin is best stored refrigerated at 4 °C.
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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.
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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.
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Dimers and aggregates: |
Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
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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.
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Endotoxin: |
Less than 0.1 ng/µg (IEU/µg) of rHuLeptin.
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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. |
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Usage |
This material is for research, laboratory or further manufacturing purposes. |