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Recombinant bovine/porcine FGF-2 (154 aa) protein (Qk056-FG)
Recombinant bovine/porcine FGF2 protein 154 aa (bFGF/basic FGF), this is the long form of FGF-2 used for the development of optimized serum-free culture media for species-specific bovine (cow) and porcine (pig) cultivated meat and veterinary research applications. Used in comparative media optimization studies with Qk040-FG porcine/bovine FGF-2 145 aa.
High quality food grade 16 kDa FGF-2 / bFGF 154 aa 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 FGF2 protein (154 aa) / bFGF (Uniprot: P03969)
>98%, by SDS-PAGE quantitative densitometry
17.1 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
Serum-free media development
bovine, porcine
species similarity:
human – 99%
Related discovery kit
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

FGF-2 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. EC50 = 85 pg/ml (5 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 Qk056 lot #104386. *Promega pGL4.33[luc2P/SRE/Hygro] #E1340
Purity

Recombinant bovine/porcine FGF2 protein (154 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 Qk056 batch #104386.
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.
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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