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High quality food grade for cultivated meat, fish, fat and dairy

Recombinant bovine/porcine FGF-2 (bFGF) 145aa protein (Qk040-FG)

Recombinant bovine/porcine FGF-2 protein 145 aa (bFGF/basic FGF) for the development of species-specific bovine (cow) and porcine (pig) cellular agriculture protocols and veterinary research applications. Can be used in comparative cell culture media optimization studies alongside Qk056, the 154aa form of porcine/bovine FGF-2.

Qkine high qualify food recombinant bovine/porcine FGF-2 protein 145 aa protein is a high purity 16 kDa protein, animal origin-free (AOF) and carrier-protein free (CF).

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1mg will be despatched as 2 x 500µg

Fast and free shipping.
Buy online with secure credit card or purchase order.
For any questions, please email orders@qkine.com

Summary

  • High purity recombinant bovine/porcine FGF-2 protein 145 aa/bFGF (Uniprot: P03969)

  • >98%, by SDS-PAGE quantitative densitometry

  • 16 kDa

  • Expressed in E. coli

  • Animal origin-free (AOF) and carrier protein-free.

  • Manufactured in our Cambridge, UK facility

  • Lyophilized from Tris/NaCl/CyS/mannitol

  • Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired, store frozen at -20 oC (short-term) or -80 oC (long-term)

Featured applications

  • Bovine and porcine stem cell expansion and maintenance; primary cell culture; cellular agriculture process development

  • Bovine and porcine primary cell culture

  • Cellular agriculture process development

Basic fibroblast growth factor, bFGF, FGFβ, FGF2, Fibroblast growth factor-basic, HBGF2

bovine, porcine

species similarity:
human – 99%

This protein has recently been reformulated and will now arrive lyophilized. This change has been made to provide enhanced stability to ensure that we offer the best customer experience in terms of shipping and storage and to align with our company sustainability goals. Please visit our reconstitution page or contact customerservice@qkine.com for further information or to request the previous datasheet.

Bioactivity

Porcine / bovine FGF-2 / bFGF Qk040 lot #104301

FGF-2 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. EC50 = 160 pg/ml (10 pM). Cells are treated in triplicate with a serial dilution of FGF-2 for 3 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data from Qk040 lot #104301. *Promega pGL4.33[luc2P/SRE/Hygro] #E1340

Purity

Porcine/bovine FGF-2 / bFGF Qk040 protein purity SDS-PAGE lot #104301

Recombinant bovine/porcine FGF-2 protein 145 aa migrates as a single major band at 16 kDa in non-reducing (NR) conditions and some dimeric protein migrating at 32 kDa. Upon reduction (R), only the 16 kDa band is visible.  No contaminating protein bands are visible. Purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.  Data from Qk040 batch #104301.

Further quality assays

  • Mass spectrometry: single species with expected mass

  • Endotoxin: <0.005 EU/μg protein (below level of detection)

  • Recovery from stock vial:  >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Protein background

Fibroblast growth factors (FGFs) are a family of growth factors which regulate a wide range of essential biological functions including cell proliferation and survival, migration and differentiation [1]. The human FGF family has 18-22 members grouped into 6-7 subfamilies based on sequence homology and phylogeny [2]. The FGF family of growth factors have critical roles during both vertebrate and invertebrate embryonic development, in adult cells they modulate tissue maintenance, wound healing and angiogenesis [1,2]. The FGF ligands bind to 4 receptors (FGFR1-4), transmembrane receptors with intracellular tyrosine kinase activity [2, 3]. Once activated FGFRs recruit Src homology-2 (SH2) or phosphotyrosine binding (PTB) domain-containing signaling proteins leading to activation of intracellular signaling pathways [1]. The main signaling pathways activated by FGF binding are the RAS/MAP kinase pathway, PI3 kinase/Akt pathway, and PLCγ pathways [1-3].

Fibroblast growth factor 2 (FGF-2) also known as basic fibroblast growth factor (bFGF) has a broad range of physiological roles including regulation of cell growth, survival and proliferation. FGF-2 is one of the FGFs which binds to and signals through all four of the FGFRs [4]. FGF-2 is an essential growth factor for the maintenance of pluripotency in human embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs) [4-6] and mesenchymal stem cells (MSCs) [7]. FGF-2 preserves pluripotency through interaction with PI3 kinase/Akt, ERK1/2, JAK/STAT and PLCγ pathways by activation of activin A. In feeder culture systems FGF-2 stimulates production of essential growth factors and cytokines from the feeder layer [7].

FGF-2 is an important factor in muscle development and healing after injury [8]. Cultured meat is a potential sustainable food generated through the in vitro myogenesis of muscle satellite (stem) cells (MSCs), involving MSC culture and differentiation, and mature muscle cell processing for flavor and texture [9]. FGF-2 induces the proliferation of cultured myoblasts and inhibits their differentiation [8, 9].

FGF-2 is an important component of Beefy9, a serum free media developed for the in vitro expansion of MSCs for cultured meat, Beefy9 allows for expansion of MSC while preserving myogenicity [10]. The two forms of recombinant bovine/porcine FGF2 protein 154 aa (Qk056-FG) and 145 aa (Qk040-FG)  available from Qkine facilitate the development of fully optimized serum-free culture media for cellular agriculture applications.

[1] Y. R. Yun, J. E. Won, E. Jeon, S. Lee, W. Kang, H. Jo, J. H. Jang, U. S. Shin, H. W. Kim, ‘Fibroblast growth factors: biology, function, and application for tissue regeneration’, J. Tissue Eng. vol. 7, pp. 2010:218142, Nov. 2010. doi: 10.4061/2010/218142

[2] Y. Xie, N. Su, J. Yang et al, ‘FGF/FGFR signaling in health and disease’, Sig. Transduct. Target. Ther. vol. 5, no. 181, 2020. doi.org/10.1038/s41392-020-00222-7

[3] A. Beenken, M. Mohammadi, ‘The FGF family: biology, pathophysiology and therapy’, Nat. Rev. Drug Discov. vol. 8, no. 3, pp. 235-53. Mar. 2009. doi: 10.1038/nrd2792

[4] M. Mossahebi-Mohammadi, M. Quan, J. S. Zhang and X. Li, ‘FGF Signaling Pathway: A Key Regulator of Stem Cell Pluripotency’, Front. Cell Dev. Biol. vol. 8, pp. 79, 2020. doi: 10.3389/fcell.2020.00079

[5] Ludwig, T. E. et al. Derivation of human embryonic stem cells in defined conditions. Nat. Biotechnol. 24, 185–187 (2006). doi.org/10.1038/nbt1177

[6] Ludwig, T. E. et al. Feeder-independent culture of human embryonic stem cells. Nat. Methods 3, 637–646 (2006). doi.org/10.1038/nmeth902

[7] Chen, G., Gulbranson, D. R., Yu, P., Hou, Z. & Thomson, J. A. Thermal stability of fibroblast growth factor protein is a determinant factor in regulating self-renewal, differentiation, and reprogramming in human pluripotent stem cells. Stem Cells 30, 623–30 (2012). doi.org/10.1002/stem.1021

[8] Bentzinger CF, von Maltzahn J, Rudnicki MA. Extrinsic regulation of satellite cell specification. Stem Cell Res Ther. 2010 Aug 26;1(3):27. doi: 10.1186/scrt27.

[9] Ahmad SS, Chun HJ, Ahmad K, Shaikh S, Lim JH, Ali S, Han SS, Hur SJ, Sohn JH, Lee EJ, Choi I. The roles of growth factors and hormones in the regulation of muscle satellite cells for cultured meat production. J Anim Sci Technol. 2023 Jan;65(1):16-31. doi: 10.5187/jast.2022.e114.

[10] Stout, A.J., Mirliani, A.B., Rittenberg, M.L. et al. Simple and effective serum-free medium for sustained expansion of bovine satellite cells for cell cultured meat. Commun Biol 5, 466 (2022). https://doi.org/10.1038/s42003-022-03423-8

Qkine high quality food grade products are intended solely for use as food processing aids, ex vivo cell manufacturing and research use. Not for direct human consumption, therapeutic or diagnostic use.
 
The authorization of novel foods, including the use of growth factors as food processing aids, is regulated by regional government agencies. The use of our products as food processing aids in novel foods requires the end-user to obtain the necessary regulatory approvals.

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