Description:
Recombinant mouse 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
Source:
E. coli
Physical Appearance:
White lyophilized (freeze-dried) powder.
Formulation:
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Solubility:
It is recommended to reconstitute the lyophilized mPRL 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.
Stability:
Lyophilized mPRL 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.
Purity:
Greater than 99.0% 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 six N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Ile-Cys-Ser
Dimers and Aggregates:
The purified mPRL (23K) consists of > 99% monomers as determined by gel-filtration chromatography.
Biological Activity:
PLR’s mPRL is fully biologically active as evidenced by inducing proliferation of Nb2 cells.
Endotoxin:
Less than 0.05 ng/µg (0.5 IEU/µg) of mPRL
Protein content:
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 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.
Usage:
This material is offered by PLR for laboratory research
