PODS™ Human FGF-2

Code Description Price Qty
PPH146-50 PODS™ Human FGF-2, 50 million £95.00
PPH146-250 PODS™ Human FGF-2, 250 million £295.00
PPH146-1000 PODS™ Human FGF-2, 1 billion £995.00

PODS™ Technology

PODS™ proteins are made using an insect cell expression system in which the active protein is co-expressed alongside polyhedrin carrier protein. Polyhedrin forms microcrystals within insect cells which specifically capture the active protein to form a co-crystal complex. The active protein is captured in its nascent, natively folded form with limited scope for proteolytic degradation. Consequently, excellent levels of bioactivity are observed. The PODS™ crystals provide a sustained release mechanism and can be used to functionalize surfaces. For further details, please refer to the PODS™ Technology page.

Product Description

The product contains the polyhedrin protein co-crystalized with Human FGF-2. 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.

Usage Recommendation

PODS™ 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. Based on previous data, we suggest using 50 million PODS™ crystals in place of 3.3 μg of standard growth factor as a 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.

AA Sequence


Alternative Names

Fibroblast Growth Factor 2, FGF2, FGF 2, HBGF-2, basic fibroblast growth factor, heparin-binding growth factor 2, FGFB, BFGF, bFGF, prostatropin
Product Details
Length 275 aa
Molecular Weight 30 kDa
Structure Monomer
Source Spodoptera frugiperda (Sf9) cell culture
Accession Number P09038
Endotoxin Level <0.06 EU/ml as measured by gel clot LAL assay
Formulation PODS™ were lyophilized from a volatile solution

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 range 6 - 8).

Stability and Storage Upon receipt, store at 4°C. PODS™ protein crystals are stable for at least 1 year when dry and 6 months when resuspended.


Hajime Mori, Chisa Shukunami, Akiko Furuyama, Hiroyuki Notsu, Yuriko Nishizaki, and Yuji Hiraki. 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.

Ijiri H, Coulibaly F, Nishimura G, Nakai D, Chiu E, Takenaka C, Ikeda K, Nakazawa H, Hamada N, Kotani E, 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.

Takatsune Shimizu, Tomoki Ishikawa, Sayaka Iwai, Arisa Ueki, Eiji Sugihara, Nobuyuki Onishi, Shinji Kuninaka, Takeshi Miyamoto, Yoshiaki Toyama, Hiroshi Ijiri, 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.

Junji Shimabukuro, Ayako Yamaoka, Ken-ichi Murata, Eiji Kotani, Tomoko Hirano, Yumiko Nakajima, Goichi Matsumoto, Hajime Mori. 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.

Kotani E, Yamamoto N, Kobayashi I, Uchino K, Muto S, Ijiri H, Shimabukuro J, Tamura T, Sezutsu H, Mori H. Cell proliferation by silk gut incorporating FGF-2 protein microcrystals. (2015) Scientific Reports. 5: 11051.

Fasséli Coulibaly, Elaine Chiu, Keiko Ikeda, Sascha Gutmann, Peter W. Haebel, Clemens Schulze-Briese, Hajime Mori, and Peter Metcalf. The molecular organization of cypovirus polyhedra. (2007) Nature. 446: 97-101.

Rey FA. Virology: Holed up in a natural crystal. (2007) Nature. 446: 35-37.

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.

Satoshi Abe, Hiroshi Ijiri, Hashiru Negishi, Hiroyuki Yamanaka, Katsuhito Sasaki, Kunio Hirata, Hajime Mori, and Takafumi Ueno. Design of Enzyme-Encapsulated Protein Containers by In-Vivo Crystal Engineering. (2015) Advanced Materials. 27(48): 7951-7956.