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

MADVAGTSNR DFRGREQRLF NSEQYNYNNS KNSRPSTSLY KKAGFAAGSP RTRGRRTEER PSGSRLGDRG RGRALPGGRL GGRGRGRAPE RVGGRGRGRG TAAPRAAPAA RGSRPGPAGT MAAGSITTLP ALPEDGGSGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHI KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTDE CFFFERLESN NYNTYRSRKY TSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS

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
Reconstitution

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.

References

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.