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. The wild type leptin was mutated at position 4 replacing arginine by cysteine. Recombinant ovine leptin R4C mutant was purified by proprietary chromatographic techniques, see Reicher et al. J. Animal Sciences 90:410-418 (2012).
Source:
E. coli
Lot Number:
Quantity Shipped:
Physical Appearance:
White lyophilized (freeze-dried) powder
Formulation:
The recombinant ovine leptin R4C mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Solubility:
It is recommended to reconstitute the lyophilized recombinant ovine leptin R4C mutant 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 R4C mutant 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 R4C mutantis 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 R4C mutant was determined and was found to be Ala-Val-Pro-Ile-Cys.
Dimers and Aggregates:
The purified recombinant ovine leptin (16K) R4C mutant consists of > 95% monomers as determined by gel-filtration chromatography.
Biological Activity:
PLR’s recombinant ovine leptin R4C mutant is fully biologically active compared to the wild-type ovine leptin 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 0.05 ng/µg (0.5 IEU/µg) of ovine leptin R4C mutant.
Protein content:
Protein quantitation of recombinant ovine leptin R4C mutant 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 R4C is offered by PLR for laboratory research
Date Shipped: