protein

Chicken prolactin (chPRL)

GHP-37

Recombinant chickenn prolactin, (chPRL) 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 as described by Oclon et al (2017) GCE 240, 27-34.

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 chPRL 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 chPRL although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution at > 0.1 chPRL mg/ml and up to 3 mg/ml and filter sterilization hPRL can be stored at 4C for several weeks.

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 six N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Ile-Cys-Pro.

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

PLR’s hPRL is biologically active as evidenced by inducing proliferation of Nb2 cells and baf/3 cells stably transfected with hPRL receptors and by in vivo in chicken.

Less than 0.1 ng/µg (IEU/µg) of hPRL

Protein content: Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.15 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

PLR's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.