FGF2, Active, Recombinant, Human (Heparin-binding Growth Factor 2, HBGF-2, Basic Fibroblast Growth Factor, bFGF, FGFB)

FGF2 is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. FGF2 is a single-chain polypeptide growth factor that plays a significant role in the process of wound healing and is a potent inducer of anguogenesis. Due to its basic pH, the factor is named FGF-2 (basic FGF, bFGF). Several different forms of the human protein exist ranging from 18-24kD in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to fibroblast growth factor 1 and has potent heparin-binding activity. 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 (fibroblast growth factor 1).\n\nSource:\nRecombinant corresponding to aa134-288 from human soluble basic FGF expressed in E.coli.\n\nMolecular Weight:\n~17kD\n\nBiological Activity:\nMeasured by its ability to stimulate proliferation of NIH3T3 cells. The ED50 of this effect is between 0.1-1ng/ml.\n\nEndotoxin: \n~1EU/ug (LAL)\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months 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

137270

Size

100ug

Form

Supplied as a lyophilized powder from 5mM Tris, pH 7.5, 150mM sodium chloride. Reconstitute with sterile buffer or dH2O.

Purity

~98% (SDS-PAGE, HPLC)

References

1. Derivation of pluripotential embryonic stem cells from murine primordial germ cells in culture. Cell 70(5), 841-847 (1992). 2. Differentiation of human embryonic stem cells into insulin-producing clusters. Stem Cells. 22(3), 265-74 (2002).