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, Recombinant ovine leptin was purified by proprietary chromatographic techniques, see Gertler et al. FEBS Lett. 442, 137-140 (1998).
Source:
Escherichia coli.
Lot Number:
Quantity Shipped:
Physical Appearance:
White lyophilized (freeze-dried) powder.
Formulation:
The recombinant ovine leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Solubility:
It is recommended to reconstitute the lyophilized recombinant ovine leptin in sterile 0.4% NaHCO3 adjusted, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability:
Lyophilized recombinant ovine leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant ovine leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant ovine leptin can be stored at 4C or even room temperature for several weeks. At lower concentration of recombinant ovine leptin addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Purity:
The purity of recombinant ovine leptin is greater than 98.0% as determined by:(a) Gel filtration analysis(b) Analysis by reducing and non-reducing SDS-PAGE gel.
Amino Acid Sequence:
The sequence of the first five N-terminal amino acids of recombinant ovine leptin was determined and was found to be Ala-Val-Pro-Ile-Arg.
Dimers and Aggregates:
The purified recombinant ovine leptin (16K) consists of > 95% monomers as determined by gel-filtration chromatography.
Biological Activity:
PLR’s recombinant ovine leptin is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
Endotoxin:
Endotoxin content of recombinant ovine leptin is less than 0.1 ng/µg (IEU/µg) of oLEP
Protein content:
Protein quantitation of recombinant ovine leptin was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
Usage:
Recombinant ovine leptin is offered by PLR for laboratory research
Date Shipped: