Certificate of Analysis & Data Sheet

Recombinant ovine placental lactogen, one polypeptide chain containing 199 amino and an additional Ala at N-terminus acids and having a molecular mass of ~ 23 kDa, was purified by proprietary chromatographic techniques (see Sakal et al. J. Endocrinology (1997), 152, 317-327. Ovine PL is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

E.coli

White lyophilized (freeze-dried) powder.

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

It is recommended to reconstitute the lyophilized oPL 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 oPL although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution at > 0.1 oPL mg/ml and up to 4 mg/ml mM and filter sterilization oPL can be stored at 4C for several weeks.

Greater than 97.0% 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 was determined and was found to be Ala-Gln-His-Pro-Pro.

The purified oPL (23K) consists of > 95% monomers as determined by gel-filtration chromatography.

PLR’s oPL is fully biologically active as evidenced by inducing proliferation of Nb2 cells.

Less than 0.1 ng/µg (IEU/µg) of oPL

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by DNAman computer analysis program of protein sequences

This material is offered by PLR for laboratory research