Certificate of Analysis & Data Sheet

Recombinant ovine prolactin, 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 Leibovich et al., Protein Expr Purif. 2001 22:489-96).

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

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by reducing and non-reducing SDS-PAGE gel.

The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro

The purified oPRL (23K) consists of > 99% monomers as determined by gel-filtration chromatography.

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

Less than 0.1 ng/µg (IEU/µg) of oPRL

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 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