Certificate of Analysis & Data Sheet

Recombinant oGHBP, one polypeptide chain containing 244 amino acids and having a molecular mass of ~ 28 kDa, hGHBP was purified by proprietary chromatographic techniques, (see Herman et al. J Biol Chem. (1999) 274, 7631-9.

Escherichia coli.

White lyophilized (freeze-dried) powder.

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

It is recommended to reconstitute the lyophilized oGHBP in DDW or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions preferably in presence of carrier proteins such as BSA or HSA.

Lyophilized oGHBP although stable at room temperature for 2 weeks, should be stored desiccated below -18C. Upon reconstitution at > 0.1 oGHBP mg/ml and filter sterilization oGHBP can be stored at 4C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

Greater than 98.0% 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-Phe-Ser-Gly-Ser.

The purified oGHBP (28K) consists of > 98% monomers as determined by gel-filtration chromatography.

PLR’s oGHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with hGH.

Less than 0.1 ng/µg (IEU/µg) of oGHBP (28 K).

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 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).

This material is offered by PLR for laboratory research.