protein

Mouse leptin

LEP-6

Recombinant mouse leptin, one polypeptide chain containing 146 amino acids and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Recombinant mouse leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purication 47, 128–136

E. coli

White lyophilized (freeze-dried) powder.

The recombinan protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

It is recommended to reconstitute the lyophilized recombinant mouse leptin in sterile water or 0.4% NaHCO3 adjusted tp pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

Lyophilized recombinant mouse leptin although stable at room temperature for several weeks, should be stored desiccated below -18 C. Upon reconstitution at > 0.1 recombinant mouse leptin mg/ml and up to 2 mg/ml and filter sterilization hLEP can be stored at +4C.

The purity of recombinant mouse leptin is greater than 95.0% as determined by: (a) Gel filtration analysis. (b) Analysis by reducing and non-reducing SDS-PAGE gel.

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

The purified recombinant mouse leptin (16K) consists of > 93% monomers as determined by gel-filtration chromatography.

PLR’s recombinant mouse leptin is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Less than 0.1 ng/µg (IEU/µg) of mouse leptin

Protein quantitation of recombinant mouse 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).

Recombinant mouse leptin is offered by PLR for laboratory research