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Recombinant Human Betacellulin produced in E.coli is a single non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of approximately 9.0KDa.
Fully biologically active when compared to standard. The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 0.05 ng/ml, corresponding to a Specific Activity of >2.0×107 IU/mg.
Less than 1EU/mg of rHuBTC as determined by LAL method.
>97% by SDS-PAGE and HPLC analyses.
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Betacellulin (BTC) is a new member of the EGF family of cytokines that is comprised of at least ten proteins including EGF, TGF-α, amphiregulin, HB-EGF, and the various heregulins. All of these cytokines are synthesized as transmembrane precursors and are characterized by the presence of one or more EGF structural units in their extracellular domain. The soluble forms of these cytokines are released by proteolytic cleavage. BTC, a heparin-binding protein, was originally isolated from the conditioned media of mouse pancreatic beta tumor cells as a 32 kDa glycoprotein composed of 80 amino acid residues. Human and mouse cDNAs encode BTC precursor proteins of 178 and 177 amino acid residues, respectively.