PODS™ Human FGF-2 crystals provide a depot of proteins which are steadily secreted. It has been estimated that the biological activity of 50 million PODS™ crystals generates the same peak dose as 3.3 µg of standard recombinant protein. However, at 5 days following the start of seeding the PODS™ crystals, there are more than 50% of these peak levels still present in the culture system. Ultimately, the amount of PODS™ crystals that is optimal for a particular experiment should be determined empirically, using 50 million PODS™ crystals equivalence to 3.3 µg of standard growth factor is a good starting point. To control for cross-reactivity with cells or as a negative control, we recommend using PODS™ growth factors alongside PODS™ Empty crystals, as the latter do not contain or release cargo protein.
- Applications:cell culture growth factors
- Applications:PODS™ protein crystals may be reconstituted at 200 million PODS™/ml in water. 20% glucose has a buoyant density closer to PODS™ protein crystals and can be useful for aliquoting. PODS™ protein crystals are highly stable when stored in aqueous solution (pH
Peptides & proteins
Fibroblast Growth Factor 2, FGF2, FGF 2, HBGF-2, basic fibroblast growth factor, heparin-binding growth factor 2, FGFB, BFGF, bFGF, prostatropin
1) Mori, H. et al. Immobilization of Bioactive Fibroblast Growth Factor-2 into Cubic Proteinous Microcrystals (Bombyx mori Cypovirus Polyhedra) That Are Insoluble in a Physiological Cellular Environment. (2007) Journal of Biological Chemistry. 282(23): 17289-17296.; 2) Ijiri H, et al. Structure-based targeting of bioactive proteins into cypovirus polyhedra and application to immobilized cytokines for mammalian cell culture. (2009) Biomaterials. 30(26): 4297-308.; 3) Shimizu, T. et al. Fibroblast Growth Factor-2 Is an Important Factor that Maintains Cellular Immaturity and Contributes to Aggressiveness of Osteosarcoma. (2012) Molecular Cancer Research. 10: 454-468.; 5) Shimabukuro, J. et al. 3D co-cultures of keratinocytes and melanocytes and cytoprotective effects on keratinocytes against reactive oxygen species by insect virus-derived protein microcrystals. (2014) Material Science and Engineering. 42: 64-69.; 6) Kotani, E. et al. Cell proliferation by silk gut incorporating FGF-2 protein microcrystals. (2015) Scientific Reports. 5: 11051.; 7) Coulibaly, F. et al. The molecular organization of cypovirus polyhedra. (2007) Nature. 446: 97-101.; 8) Rey FA. Virology: Holed up in a natural crystal. (2007) Nature. 446: 35-37.; 9) Mori H. Immobilization of Bioactive Growth Factors into Cubic Proteinous Microcrystals (Cypovirus Polyhedra) and Control of Cell Proliferation and Differentiation. (2010) NSTI-Nanotech. 3: 222-225.; 10) Abe, S. et al. Design of Enzyme-Encapsulated Protein Containers by In-Vivo Crystal Engineering. (2015) Advanced Materials. 27(48): 7951-7956.
Upon receipt, store at 4°C. PO
SOURCE: Spodoptera frugiperda (Sf9) cell culture; LENGTH: 275 aa; STRUCTURE: Monomer; FORMAT: lyophilized; ENDOTOXIN LEVEL: <0.06 EU/ml as measured by gel clot LAL assay; BACKGROUND: Fibroblast Growth Factor 2 (FGF-2) is expressed by endothelial cells and is a mediator of angiogenesis. FGF-2 also has cardioprotective functions during heart injury. The application of FGF-2 is a critical component for embryonic stem cell culture systems and is necessary for maintaining cells in an undifferentiated state. Degredation of the full length FGF-2 N-terminus results in a truncated FGF-2 147 amino acids protein, when the protein is isolated from biological sources. The N-terminus extensions influence the localization of FGF-2 within the cell, but do not affect the biological activity of FGF-2.