Fibroblast Growth Factor-Basic; Human FGF-Basic, 1mg

FGF-basic, Fibroblast Growth Factor-basic, human: Human Fibroblast Growth Factor-basic FGF basic (FGF-2, HBGF-2) is one of at least 22 mitogenic proteins of the FGF family, which show 35 - 60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans (HSPG) are likely. The predicted 17 kDa FGF basic isoform can be located in both the cytoplasm and the nucleus and is presumed to be the form secreted. Transcription from alternate start sites produces 21 - 24 kDa forms found only in the nucleus. High and low molecular weight human FGF basic targets the expression of different genes when expressed in NIH-3T3 cells. Recombinant Human Fibroblast Growth Factor-basic (rHuFGF-2 ) Source: Escherichia coli.  Molecular Weight:  Approximately 17.3 kDa, a single non-glycosylated polypeptide chain containing 155 amino acids.  Quantity: 10ug/50ug/1000µg Purity: >96% by SDS-PAGE and HPLC analyses.  Biological Activity:  Fully biologically active when compared to standard. The ED50, calculated by the dose- dependant proliferation of BAF3 cells  expressing FGF  receptors  (measured  by 3H- thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2.0 x 106 Units/mg.  Formulation: Lyophilized from a 0.2?m filtered concentrated (1mg/ml) solution in PBS, pH 7.4. AA Sequence: MPALPEDGGAAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHVKLQLQAEERGVV SIKGVCANRYLAMKEDGRLLASKCVTEECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGSK TGPGQKAILFLPMSAKS Endotoxin level: Less than 1EU/?g of rHubFGF as determined by LAL method. Reconstitution: 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.