Fibroblast Growth Factor, Basic, Recombinant, Bovine (FGFb)

Single-chain polypeptide growth factor that plays a significant role in the process of wound healing and is a potent inducer of angiogenesis. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor. \n\nRecombinant Bovine FGF-b (FGF-2) is a single, non-glycosylated, polypeptide chain containing 155 amino acids having a molecular mass of 17,250D. \n\nSequence:\nThe sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Ala-Gly-Ser.\n\nProtein Content:\nProtein quantitation was carried out by two independent methods: \n1. UV spectroscopy at 280nm. \n2. Analysis by RP-HPLC, using a standard solution of FGF-b as a Reference Standard. \n\nBiological Activity:\nrbFGF-b is fully biologically active when compared to standards. The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be less then 0.1ng/ml, corresponding to a specific activity of 3x10e6 Units/mg. \n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

F4210-20B

Size

10ug

Form

Supplied as a lyophilized powder from 1% HSA. Reconstitute in sterile ddH2O to a concentration of >0.1mg/ml.

Purity

(same/more than) 97% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.

References

1. Talbot NC, Powell AM, Cloning Stem Cells 6(1):37-47 (2004). 2. Neuvians TP, Berisha B, Mol Reprod Dev Apr;67( 4):389-95 (2004) .3. Sun ZH, Yao K, Wu RY, Zhonghua Yan Ke Za Zhi 2003 Nov;39(11):694-7 4. Berisha B, Sinowatz F, Mol Reprod Dev 2004 Feb;67(2):162-71 5.Neuvians TP, Schams D, Pfaffl MW, Biol Reprod 2004 Feb;70(2):473-80 6 Saito S, Sawai K, Moriyasu S, Kageyama S, Biochem Biophys Res Commun 2003 Sep 12;309(1):104-13.